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dark operative protochlorophyllide oxidoreductase
dark protochlorophyllide reductase
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dark-operative Pchlide oxidoreductase
dark-operative protochlorophyllide oxidoreductase
dark-operative protochlorophyllide reductase
light-independent (dark) Pchlide reductase
-
light-independent (dark-operative) Pchlide oxidoreductase
light-independent Pchlide oxidoreductase
light-independent Pchlide reductase
light-independent protochlorophyllide oxidoreductase
light-independent protochlorophyllide oxidoreductases
-
light-independent protochlorophyllide reductase
protochlorophyllide oxidoreductase
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-
protochlorophyllide oxidoreductase complex
-
bchB
-
bchL
-
bchN
-
dark operative protochlorophyllide oxidoreductase
-
-
dark operative protochlorophyllide oxidoreductase
Thermosynechococcus vestitus
-
-
dark-operative Pchlide oxidoreductase
-
-
dark-operative Pchlide oxidoreductase
-
-
dark-operative Pchlide oxidoreductase
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-
dark-operative Pchlide oxidoreductase
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dark-operative Pchlide oxidoreductase
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dark-operative Pchlide oxidoreductase
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-
dark-operative Pchlide oxidoreductase
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dark-operative protochlorophyllide oxidoreductase
-
dark-operative protochlorophyllide oxidoreductase
-
dark-operative protochlorophyllide oxidoreductase
-
dark-operative protochlorophyllide oxidoreductase
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dark-operative protochlorophyllide oxidoreductase
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dark-operative protochlorophyllide reductase
-
dark-operative protochlorophyllide reductase
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DPOR
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DPOR
the DPOR holoenzyme is comprised of two component proteins, the dimeric protein L and the heterotetrameric NB-protein
DPOR
-
DPOR consists of two components, the L-protein and the NB-protein
DPOR
Thermosynechococcus vestitus
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-
light-independent (dark-operative) Pchlide oxidoreductase
-
-
light-independent (dark-operative) Pchlide oxidoreductase
-
-
-
light-independent Pchlide oxidoreductase
-
light-independent Pchlide oxidoreductase
-
light-independent Pchlide oxidoreductase
-
-
light-independent Pchlide reductase
-
-
light-independent Pchlide reductase
-
light-independent Pchlide reductase
-
-
light-independent protochlorophyllide oxidoreductase
-
light-independent protochlorophyllide oxidoreductase
-
-
light-independent protochlorophyllide oxidoreductase
-
-
light-independent protochlorophyllide reductase
-
light-independent protochlorophyllide reductase
-
light-independent protochlorophyllide reductase
-
-
light-independent protochlorophyllide reductase
-
-
light-independent protochlorophyllide reductase
-
-
light-independent protochlorophyllide reductase
-
light-independent protochlorophyllide reductase
-
-
-
light-independent protochlorophyllide reductase
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate = protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate = protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
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-
-
-
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate = protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
reaction mechanism for trans-specific reduction, overview
-
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate = protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
dynamic switch mechanism of DPOR, catalytic mechanism and structure-function analysis, detailed overview
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate = protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
reaction mechanism and structure-function relationship, overview
-
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate = protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
reaction mechanism and structure-function relationship, overview
-
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate = protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
reaction mechanism and structure-function relationship, overview
-
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate = protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
reaction mechanism and structure-function relationship, overview
-
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate = protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
reaction mechanism and structure-function relationship, overview
-
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate = protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
reaction mechanism and structure-function relationship, overview
-
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate = protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
reaction mechanism for trans-specific reduction, overview
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-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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chlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
protochlorophyllide + oxidized ferredoxin + 2 ADP + 2 phosphate + 2 H+
chlorophyllide a + reduced ferredoxin + ATP
protochlorophyllide + oxidized ferredoxin + ADP + phosphate
protochlorophyllide + oxidized ferredoxin + ADP + phosphate
chlorophyllide a + reduced ferredoxin + ATP
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
protochlorophyllide a + reduced ferredoxin + 4 ATP + 4 H2O
chlorophyllide a + oxidized ferredoxin + 4 ADP + 4 phosphate
additional information
?
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chlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
protochlorophyllide + oxidized ferredoxin + 2 ADP + 2 phosphate + 2 H+
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-
-
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?
chlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
protochlorophyllide + oxidized ferredoxin + 2 ADP + 2 phosphate + 2 H+
-
-
-
-
?
chlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
protochlorophyllide + oxidized ferredoxin + 2 ADP + 2 phosphate + 2 H+
Thermosynechococcus vestitus
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-
-
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?
chlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
protochlorophyllide + oxidized ferredoxin + 2 ADP + 2 phosphate + 2 H+
Thermosynechococcus vestitus
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ferredoxin provides a single electron to ChlL2, which in turn transfers an electron to (ChlN/ChlB)2. Hydrolysis of the two ATP molecules results in the dissociation of ChlL2 from reduced (ChlN/ChlB)2. Protochlorophyllide reduction is completed after two sequential catalytic redox cycles. Substrate recognition by (ChlN/ChlB)2 essentially involves all functional groups of the substrate, modeling of the substrate binding site of (ChlN/ChlB)2, overview. Electron transfer pathway via the various redox centers of DPOR to the substrate, overview
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?
chlorophyllide a + reduced ferredoxin + ATP
protochlorophyllide + oxidized ferredoxin + ADP + phosphate
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-
?
chlorophyllide a + reduced ferredoxin + ATP
protochlorophyllide + oxidized ferredoxin + ADP + phosphate
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-
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-
?
chlorophyllide a + reduced ferredoxin + ATP
protochlorophyllide + oxidized ferredoxin + ADP + phosphate
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?
protochlorophyllide + oxidized ferredoxin + ADP + phosphate
chlorophyllide a + reduced ferredoxin + ATP
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-
?
protochlorophyllide + oxidized ferredoxin + ADP + phosphate
chlorophyllide a + reduced ferredoxin + ATP
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?
protochlorophyllide + oxidized ferredoxin + ADP + phosphate
chlorophyllide a + reduced ferredoxin + ATP
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?
protochlorophyllide + oxidized ferredoxin + ADP + phosphate
chlorophyllide a + reduced ferredoxin + ATP
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-
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-
?
protochlorophyllide + oxidized ferredoxin + ADP + phosphate
chlorophyllide a + reduced ferredoxin + ATP
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-
-
?
protochlorophyllide + oxidized ferredoxin + ADP + phosphate
chlorophyllide a + reduced ferredoxin + ATP
-
DPOR catalyzes the stereo-specific reduction of C17-C18 double bond on the D-ring of protochlorophyllide
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?
protochlorophyllide + oxidized ferredoxin + ADP + phosphate
chlorophyllide a + reduced ferredoxin + ATP
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-
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?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
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?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
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?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
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?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
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?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
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?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
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?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
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?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
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?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
DPOR catalyzes the formation of chlorophyllide a through ATP-dependent, stereospecific reduction of the C-17=C-18 double bond of Pchlide ring D
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?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
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the homodimeric ChlL2 subunit carrying a [4Fe-4S] cluster transfers electrons to the corresponding heterotetrameric catalytic subunit (ChlN/ChlB)2, which also possesses a redox active [4Fe-4S] cluster
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?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
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?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
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-
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?
protochlorophyllide a + reduced ferredoxin + 4 ATP + 4 H2O
chlorophyllide a + oxidized ferredoxin + 4 ADP + 4 phosphate
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?
protochlorophyllide a + reduced ferredoxin + 4 ATP + 4 H2O
chlorophyllide a + oxidized ferredoxin + 4 ADP + 4 phosphate
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?
additional information
?
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proposed catalytic redox cycle of DPOR, overview
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-
?
additional information
?
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although chlorophyllide c binds to the substrate-binding pocket in the NB-protein, the C17-C18 double bond on the D-ring of chlorophyllide c is not reduced by the DPOR
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?
additional information
?
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DPOR is a nitrogenase-like enzyme consisting of two components, L-protein (a BchL dimer) and NB-protein (a BchN-BchB heterotetramer)
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?
additional information
?
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each catalytic BchN-BchB unit contains one protochlorophyllidee and one iron-sulfur NB-cluster coordinated uniquely by one aspartate and three cysteines. Unique aspartate ligation is not necessarily needed for the cluster assembly but is essential for the catalytic activity. Specific protochlorophyllide-binding accompanies the partial unwinding of an alpha-helix that belongs to the next catalytic BchN-BchB unit, unique trans-specific reduction mechanism in which the distorted C17-propionate of protochlorophyllid and an aspartate from BchB serve as proton donors for C18 and C17 of protochlorophyllide, respectively, overview
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?
additional information
?
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the C175C18 double bond of chlorophyll c is not reduced by DPOR
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?
additional information
?
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The reaction mechanism begins with single-electron reduction of the substrate by the (Cys)3Asp-ligated [4Fe-4S]-center, yielding a negatively-charged intermediate. Depending on the rate of Fe-S cluster re-reduction, the reaction either proceeds through double protonation of the single-electron-reduced substrate, or by alternating proton/electron transfer. The Fe-S cluster rereduction should be the rate-limiting stage of the process
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?
additional information
?
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The reaction mechanism begins with single-electron reduction of the substrate by the (Cys)3Asp-ligated [4Fe-4S]-center, yielding a negatively-charged intermediate. Depending on the rate of Fe-S cluster re-reduction, the reaction either proceeds through double protonation of the single-electron-reduced substrate, or by alternating proton/electron transfer. The Fe-S cluster rereduction should be the rate-limiting stage of the process
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?
additional information
?
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DPOR is a nitrogenase-like enzyme consisting of two components, L-protein (a BchL dimer) and NB-protein (a BchN-BchB heterotetramer)
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?
additional information
?
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each catalytic BchN-BchB unit contains one protochlorophyllidee and one iron-sulfur NB-cluster coordinated uniquely by one aspartate and three cysteines. Unique aspartate ligation is not necessarily needed for the cluster assembly but is essential for the catalytic activity. Specific protochlorophyllide-binding accompanies the partial unwinding of an alpha-helix that belongs to the next catalytic BchN-BchB unit, unique trans-specific reduction mechanism in which the distorted C17-propionate of protochlorophyllid and an aspartate from BchB serve as proton donors for C18 and C17 of protochlorophyllide, respectively, overview
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?
additional information
?
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the C175C18 double bond of chlorophyll c is not reduced by DPOR
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?
additional information
?
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Thermosynechococcus vestitus
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the invitro assay is performed with purified recombinant GST-tagged (ChlN/ChlB)2 complex and a ChlL2 subunit purified from Prochlorococcus marinus
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chlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
protochlorophyllide + oxidized ferredoxin + 2 ADP + 2 phosphate + 2 H+
chlorophyllide a + reduced ferredoxin + ATP
protochlorophyllide + oxidized ferredoxin + ADP + phosphate
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-
?
protochlorophyllide + oxidized ferredoxin + ADP + phosphate
chlorophyllide a + reduced ferredoxin + ATP
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
additional information
?
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proposed catalytic redox cycle of DPOR, overview
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?
chlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
protochlorophyllide + oxidized ferredoxin + 2 ADP + 2 phosphate + 2 H+
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?
chlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
protochlorophyllide + oxidized ferredoxin + 2 ADP + 2 phosphate + 2 H+
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-
-
?
chlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
protochlorophyllide + oxidized ferredoxin + 2 ADP + 2 phosphate + 2 H+
Thermosynechococcus vestitus
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?
protochlorophyllide + oxidized ferredoxin + ADP + phosphate
chlorophyllide a + reduced ferredoxin + ATP
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?
protochlorophyllide + oxidized ferredoxin + ADP + phosphate
chlorophyllide a + reduced ferredoxin + ATP
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?
protochlorophyllide + oxidized ferredoxin + ADP + phosphate
chlorophyllide a + reduced ferredoxin + ATP
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?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
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?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
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?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
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-
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?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
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?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
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-
?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
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?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
-
-
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-
?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
-
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-
?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
-
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-
?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
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-
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?
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SwissProt
brenda
subunit B, subunit L, and subunit N; strain CS-41, also named Auxenochlorella protothecoides strain CS-41
UniProt
brenda
subunit B, subunit L, and subunit N
UniProt
brenda
subunit B, subunit L, and subunit N
UniProt
brenda
subunit B, subunit L, and subunit N
UniProt
brenda
three subunits of DPOR, encoded by genes bchL, bchN and bchB
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-
brenda
three subunits of DPOR, encoded by genes bchL, bchN and bchB
-
-
brenda
subunit B, subunit L, and subunit N
UniProt
brenda
subunit B, subunit L, and subunit N
UniProt
brenda
subunit B, subunit L, and subunit N
UniProt
brenda
subunit B, subunit L, and subunit N
UniProt
brenda
three subunits of DPOR, encoded by genes bchL, bchN and bchB
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-
brenda
subunit B, subunit L, and subunit N; variant Juniperus chinensis procumbens
UniProt
brenda
subunit B, subunit L and subunit N
UniProt
brenda
subunit B, subunit L, and subunit N
UniProt
brenda
no activity in Hordeum vulgare
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-
-
brenda
no activity in Thuja occidentalis
-
-
-
brenda
no activity in Thuja plicata
-
-
-
brenda
no activity in Thuja standishii
-
-
-
brenda
gene chlB; three constitutive plastid genes chlL, chlN, and chlB
UniProt
brenda
gene chlB; three constitutive plastid genes chlL, chlN, and chlB
UniProt
brenda
loblolly pine
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brenda
gene chlB encoding the ChlB subunit of the enzyme complex
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brenda
subunit B, subunit L and subunit N
UniProt
brenda
-
-
-
brenda
subunit bchL
UniProt
brenda
subunit B, subunit L, and subunit N
UniProt
brenda
subunit B, subunit L, and subunit N
UniProt
brenda
-
-
-
brenda
subunit B, subunit L, and subunit N
UniProt
brenda
Thermosynechococcus vestitus
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brenda
-
UniProt
brenda
three subunits of DPOR, encoded by genes bchL, bchN and bchB
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brenda
-
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-
brenda
strain IAM-M101
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brenda
DPOR subunit B; strain UTEX 481, also called Calothrix sp. PCC 7601 and Tolypothrix sp. PCC 7601
UniProt
brenda
DPOR subunit L; strain UTEX 481, also called Calothrix sp. PCC 7601 and Tolypothrix sp. PCC 7601
UniProt
brenda
DPOR subunit N; strain UTEX 481, also called Calothrix sp. PCC 7601 and Tolypothrix sp. PCC 7601
UniProt
brenda
-
-
-
brenda
-
UniProt
brenda
three subunits of DPOR, encoded by genes bchL, bchN and bchB
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brenda
-
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brenda
D5ANS3 i.e. iron-sulfur ATP-binding protein BchL, P26164 i.e. subunit BchN, P26163 i.e. reductase subunit BchB
UniProt
brenda
strain strain CB1029
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-
brenda
subunit bchB; strain SB1003
UniProt
brenda
subunit bchL
UniProt
brenda
subunit bchN
UniProt
brenda
subunit bchN; strain SB1003
UniProt
brenda
three subunits of DPOR, encoded by genes bchL, bchN and bchB
-
-
brenda
D5ANS3 i.e. iron-sulfur ATP-binding protein BchL, P26164 i.e. subunit BchN, P26163 i.e. reductase subunit BchB
UniProt
brenda
subunit bchN
UniProt
brenda
subunit B
UniProt
brenda
subunit L
UniProt
brenda
subunit N
UniProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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malfunction
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a strain lacking DPOR contains about 25% of the wild-type level of photosystems PSII and PSI when cultivated under light-activated heterotrophic growth conditions. Deletion of the chlL gene abolishes activity of the DPOR enzyme. Absence of the chlL gene causes a further 20% decrease in Chl content and therefore the resulting (pCER:por)/Dpor/DchlL strain termed SynPORreg reaches only 60-70% of Chl content present in wild-type
evolution
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cyanobacteria, algae, bryophytes, pteridophytes and gymnosperms use an additional, light-independent enzyme dubbed dark-operative Pchlide oxidoreductase for chlorophyll biosynthesis, besides a light-dependent enzyme, mechanisms of protochlorophyllide a reduction in photosynthetic organisms, ooverview
evolution
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cyanobacteria, algae, bryophytes, pteridophytes and gymnosperms use an additional, light-independent enzyme dubbed dark-operative Pchlide oxidoreductase for chlorophyll biosynthesis, besides a light-dependent enzyme, mechanisms of protochlorophyllide a reduction in photosynthetic organisms, ooverview
evolution
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cyanobacteria, algae, bryophytes, pteridophytes and gymnosperms use an additional, light-independent enzyme dubbed dark-operative Pchlide oxidoreductase for chlorophyll biosynthesis, besides a light-dependent enzyme, mechanisms of protochlorophyllide a reduction in photosynthetic organisms, ooverview
evolution
-
cyanobacteria, algae, bryophytes, pteridophytes and gymnosperms use an additional, light-independent enzyme dubbed dark-operative Pchlide oxidoreductase for chlorophyll biosynthesis, besides a light-dependent enzyme, mechanisms of protochlorophyllide a reduction in photosynthetic organisms, ooverview
evolution
-
cyanobacteria, algae, bryophytes, pteridophytes and gymnosperms use an additional, light-independent enzyme dubbed dark-operative Pchlide oxidoreductase for chlorophyll biosynthesis, besides a light-dependent enzyme, mechanisms of protochlorophyllide a reduction in photosynthetic organisms, ooverview
evolution
-
cyanobacteria, algae, bryophytes, pteridophytes and gymnosperms use an additional, light-independent enzyme dubbed dark-operative Pchlide oxidoreductase for chlorophyll biosynthesis, besides a light-dependent enzyme, mechanisms of protochlorophyllide a reduction in photosynthetic organisms, overview
evolution
protein-protein interaction surfaces for transition state complexes of DPOR and nitrogenase, using PDB ID code 1M34, analysis of catalytic differences and similarities between DPOR and nitrogenase, overview
evolution
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the enzyme is involved in the biosynthesis of chlorophylls and bacteriochlorophylls in gymnosperm, ferns, algae, and photosynthetic bacteria
metabolism
-
chlorophyll biosynthesis is catalyzed by two multi subunit enzymes; a light-dependent and a light-independent protochlorophyllide oxidoreductase
metabolism
protochlorophyllide reduction is a key regulatory step in Chl biosynthesis
metabolism
protochlorophyllide reduction is a key regulatory step in Chl biosynthesis
metabolism
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the three-subunit enzyme dubbed DPOR operates in the synthesis of Bchls a, b, and g
metabolism
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the three-subunit enzyme dubbed DPOR operates in the synthesis of Bchls a, b, and g
metabolism
-
the three-subunit enzyme dubbed DPOR operates in the synthesis of Bchls a, b, and g
metabolism
-
the three-subunit enzyme dubbed DPOR operates in the synthesis of Bchls a, b, and g
metabolism
-
two independent enzymes catalyze the reduction of protochlorophyllide to chlorophyllide, which is the penultimate step in chlorophyll biosynthesis. One is light-dependent NADPH:protochlorophyllide oxidoreductase and the second type is dark-operative protochlorophyllide oxidoreductase
physiological function
-
DPOR is a determinant enzyme for greening ability in the dark
physiological function
-
DPOR performs reduction of the C17-C18 double bond of protochlorophyllide to form chlorophyllide a, the direct precursor of chlorophyll a in a light-independent, dark-operative way of action
physiological function
DPOR plays a key role in the ability to synthesize chlorophyll in darkness
physiological function
DPOR plays a key role in the ability to synthesize chlorophyll in darkness
physiological function
DPOR plays a key role in the ability to synthesize chlorophyll in darkness
physiological function
DPOR plays a key role in the ability to synthesize chlorophyll in darkness
physiological function
DPOR plays a key role in the ability to synthesize chlorophyll in darkness
physiological function
DPOR plays a key role in the ability to synthesize chlorophyll in darkness
physiological function
DPOR plays a key role in the ability to synthesize chlorophyll in darkness
physiological function
DPOR plays a key role in the ability to synthesize chlorophyll in darkness
physiological function
DPOR plays a key role in the ability to synthesize chlorophyll in darkness
physiological function
DPOR plays a key role in the ability to synthesize chlorophyll in darkness
physiological function
DPOR plays a key role in the ability to synthesize chlorophyll in darkness
physiological function
DPOR plays a key role in the ability to synthesize chlorophyll in darkness
physiological function
DPOR plays a key role in the ability to synthesize chlorophyll in darkness
physiological function
DPOR plays a key role in the ability to synthesize chlorophyll in darkness
physiological function
DPOR plays a key role in the ability to synthesize chlorophyll in darkness
physiological function
light-independent protochlorophyllide reductase is required for protochlorophyllide reduction in the dark
physiological function
during chlorophyll biosynthesis in photosynthetic bacteria, cyanobacteria, green algae and gymnosperms, dark-operative protochlorophyllide oxidoreductase, a nitrogenase-like metalloenzyme, catalyzes the chemically challenging two-electron reduction of the fully conjugated ring system of protochlorophyllide a. The reduction of the C-17=C-18 double bond results in the characteristic ring architecture of all chlorophylls, thereby altering the absorption properties of the molecule and providing the basis for light-capturing and energytransduction processes of photosynthesis
physiological function
the expression of NADPH:protochlorophyllide oxidoreductase A (PorA), PorB, and PorC, which catalyze a key step in chlorophyll biosynthesis, is increased in the BRM mutants, defective in a SWI2/SNF2 chromatin-remodeling ATPase
physiological function
-
DPOR performs reduction of the C17-C18 double bond of protochlorophyllide to form chlorophyllide a, the direct precursor of chlorophyll a in a light-independent, dark-operative way of action
-
additional information
dark-grown seedlings of Pinus mugo accumulate chlorophyll and its precursor protochlorophyllide
additional information
dark-grown seedlings of Pinus sylvestris accumulate chlorophyll and its precursor protochlorophyllide
additional information
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some purple bacteria contain Bchl b, and heliobacteria such as Heliobacillus mobilis contain Bchl g, as compared to Chl a and Chl b of higher plants
additional information
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the homodimeric subunit ChlL2 transfers electrons to the corresponding heterotetrameric catalytic subunit (ChlN/ChlB)2, transfer of a single electron from the [4Fe-4S] cluster of ChlL2 onto a second [4Fe-4S] cluster located on (ChlN/ChlB)2
additional information
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the organism contains another type of Chl, bacteriochlorophyll (Bchl) a, as compared to Chl a and Chl b of higher plants
additional information
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the organism contains another type of Chl, bacteriochlorophyll (Bchl) a, as compared to Chl a and Chl b of higher plants
additional information
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the organism contains another type of Chl, bacteriochlorophyll (Bchl) a, as compared to Chl a and Chl b of higher plants. Residue Asp36 is not necessary for enzyme complex formation but for enzyme activity. Subunit BchB possesses a unique C-terminal region consisting of approximately 100 amino acid residues (Phe422-Arg525), which is probably important for protochlorophyllide reduction
additional information
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transient protein-protein interaction of ChlL2 and (ChlN/ChlB)2 is essential for the ATP-dependent electron transfer processes catalyzed by DPOR. Efficient octameric (ChlN/ChlB)2(ChlL2)2 enzyme complex formation required the presence of protochlorophyllide. Complete ATP hydrolysis is a prerequisite for intersubunit electron transfer
additional information
upon complex formation, substantial ATP-dependent conformational rearrangements of L2 trigger the protein-protein interactions with (NB)2 as well as the electron transduction via redox-active [4Fe-4S] clusters, dynamic interplay between L2 and (NB)2. Asp155 is responsible for positioning and/or activating a specific water molecule for the subsequent ATP hydrolysis, whereas Lys37 of the P-loop possibly assists the release of gamma-phosphate upon ATP hydrolysis
additional information
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upon complex formation, substantial ATP-dependent conformational rearrangements of L2 trigger the protein-protein interactions with (NB)2 as well as the electron transduction via redox-active [4Fe-4S] clusters, dynamic interplay between L2 and (NB)2. Asp155 is responsible for positioning and/or activating a specific water molecule for the subsequent ATP hydrolysis, whereas Lys37 of the P-loop possibly assists the release of gamma-phosphate upon ATP hydrolysis
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200000
-
NB-protein complex, gel filtration
31000
-
2 * 31000, L-protein of DPOR, SDS-PAGE
33310
calculated from amino acid sequence
33413
-
2 * 33413, L-protein of DPOR, calculated from amino acid sequence
35000
-
octameric (ChlN/ChlB)2(ChlL2)2 subunit complex, 4 * 35000, subunit ChlL, + 2 * 45000, subunit ChlN, 2 * 60000, subunit ChlB, SDS-PAGE, 4 * 32395,subunit ChlL, + 2 * 46199, subunit ChlN, 2 * 58729, subunit ChlB, sequence calculation
36000
-
2 * 36000, S-tag subunit BchL, SDS-PAGE
360000
-
enzyme complex, gel filtration
36046
-
2 * 36046, subunit BchL calculated from amino acid sequence
38000
1 * 38000 + 1 * 49000 + 1 * 58000, SDS-PAGE
43000
-
2 * 51000 + 2 * 43000 , NB-protein of DPOR, SDS-PAGE
45000
-
octameric (ChlN/ChlB)2(ChlL2)2 subunit complex, 4 * 35000, subunit ChlL, + 2 * 45000, subunit ChlN, 2 * 60000, subunit ChlB, SDS-PAGE, 4 * 32395,subunit ChlL, + 2 * 46199, subunit ChlN, 2 * 58729, subunit ChlB, sequence calculation
46038
-
2 * 57191 + 2 * 46038, NB-protein of DPOR, calculated from amino acid sequence
46199
-
octameric (ChlN/ChlB)2(ChlL2)2 subunit complex, 4 * 35000, subunit ChlL, + 2 * 45000, subunit ChlN, 2 * 60000, subunit ChlB, SDS-PAGE, 4 * 32395,subunit ChlL, + 2 * 46199, subunit ChlN, 2 * 58729, subunit ChlB, sequence calculation
48671
-
2 * 48671 + 2 * 57191, subunit BchN and subunit BchB, calculated from amino acid sequence
49000
1 * 38000 + 1 * 49000 + 1 * 58000, SDS-PAGE
51000
-
2 * 51000 + 2 * 43000 , NB-protein of DPOR, SDS-PAGE
52000
-
2 * 52000 + 2 * 60000, NB-protein complex, SDS-PAGE
56820
-
subunit ChlB, calculated from amino acid sequence
58729
-
octameric (ChlN/ChlB)2(ChlL2)2 subunit complex, 4 * 35000, subunit ChlL, + 2 * 45000, subunit ChlN, 2 * 60000, subunit ChlB, SDS-PAGE, 4 * 32395,subunit ChlL, + 2 * 46199, subunit ChlN, 2 * 58729, subunit ChlB, sequence calculation
67000
-
S-tag subunit BchL, gel filtration
57191
-
2 * 48671 + 2 * 57191, subunit BchN and subunit BchB, calculated from amino acid sequence
57191
-
2 * 57191 + 2 * 46038, NB-protein of DPOR, calculated from amino acid sequence
58000
-
His-tagged subunit ChlB fusion protein, SDS-PAGE
58000
1 * 38000 + 1 * 49000 + 1 * 58000, SDS-PAGE
60000
-
2 * 52000 + 2 * 60000, NB-protein complex, SDS-PAGE
60000
-
octameric (ChlN/ChlB)2(ChlL2)2 subunit complex, 4 * 35000, subunit ChlL, + 2 * 45000, subunit ChlN, 2 * 60000, subunit ChlB, SDS-PAGE, 4 * 32395,subunit ChlL, + 2 * 46199, subunit ChlN, 2 * 58729, subunit ChlB, sequence calculation
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heterodimer
1 * 38000 + 1 * 49000 + 1 * 58000, SDS-PAGE
heterooctamer
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(alpha2)2(betagamma)4, DPOR is a nitrogenase-like enzyme consisting of two components, L-protein, a BchL dimer, and NB-protein, a BchN-BchB heterotetramer, which are structurally related to nitrogenase Fe protein and MoFe protein, respectively
heterooctamer
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(alpha2)2(betagamma)4, DPOR is a nitrogenase-like enzyme consisting of two components, L-protein, a BchL dimer, and NB-protein, a BchN-BchB heterotetramer, which are structurally related to nitrogenase Fe protein and MoFe protein, respectively
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heterooctamer
Thermosynechococcus vestitus
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(alpha2)2(betagamma)4, DPOR is composed of the subunits ChlL, ChlN, and ChlB. Homodimeric ChlL2 bearing an intersubunit [4Fe-4S] cluster is an ATP-dependent reductase transferring single electrons to the heterotetrameric (ChlN/ChlB)2 complex. The latter contains two intersubunit [4Fe-4S] clusters and two protochlorophyllide binding sites, respectively, structure analysis of the catalytic (ChlN/ChlB)2 complex, overview. Subunits ChlN and ChlB exhibit a related architecture of three subdomains each built around a central, parallel beta-sheet surrounded by alpha-helices. Two ChlL2 dimers simultaneously interact with the (ChlN/ChlB)2 tetramer, giving rise to a heterooctameric holoenzyme
heterotetramer
-
2 * 48671 + 2 * 57191, subunit BchN and subunit BchB, calculated from amino acid sequence
heterotetramer
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2 * 51000 + 2 * 43000 , NB-protein of DPOR, SDS-PAGE
heterotetramer
-
2 * 52000 + 2 * 60000, NB-protein complex, SDS-PAGE
heterotetramer
-
2 * 57191 + 2 * 46038, NB-protein of DPOR, calculated from amino acid sequence
homodimer
-
2 * 31000, L-protein of DPOR, SDS-PAGE
homodimer
-
2 * 33413, L-protein of DPOR, calculated from amino acid sequence
homodimer
-
2 * 36000, S-tag subunit BchL, SDS-PAGE
homodimer
-
2 * 36046, subunit BchL calculated from amino acid sequence
octamer
(L2)2(NB)2 enzyme complex with perfect symmetry. Subunits L2 and NifH2 both contain a subunit-bridging [4Fe-4S] cluster, whereas the [4Fe-4S] cluster at the N/B subunit interface of (NB)2 is located in an analogous position as the [8Fe-7S] P-cluster at the NifD/NifK subunit interface of (NifDK)2
octamer
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octameric (ChlN/ChlB)2(ChlL2)2 subunit complex, 4 * 35000, subunit ChlL, + 2 * 45000, subunit ChlN, 2 * 60000, subunit ChlB, SDS-PAGE, 4 * 32395,subunit ChlL, + 2 * 46199, subunit ChlN, 2 * 58729, subunit ChlB, sequence calculation
octamer
-
octameric (ChlN/ChlB)2(ChlL2)2 subunit complex, with homodimeric subunit ChlL2 and heterotetrameric catalytic subunit (ChlN/ChlB)2
additional information
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DPOR consists of two components: a reductase component designated L-protein (a BchL dimer) and a catalytic component named NB-protein (a BchNĀBchB heterotetramer), structure analysis and comparison to the nitrogenase complex, overview
additional information
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DPOR consists of two components: a reductase component designated L-protein (a BchL dimer) and a catalytic component named NB-protein (a BchN-BchB heterotetramer), structure analysis and comparison to the nitrogenase complex, overview
additional information
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DPOR consists of two components: a reductase component designated L-protein (a BchL dimer) and a catalytic component named NB-protein (a BchN-BchB heterotetramer), structure analysis and comparison to the nitrogenase complex, overview
additional information
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DPOR consists of two components: a reductase component designated L-protein (a BchL dimer) and a catalytic component named NB-protein (a BchN-BchB heterotetramer), structure analysis and comparison to the nitrogenase complex, overview
additional information
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the light-independent enzyme consists of three subunit types, ChlL, ChlN and ChlB. ChlB in photosynthetic bacteria and plastids is the major subunit that catalyzes the reduction of protochlorophyllide to chlorophyllide
additional information
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DPOR consists of two components: a reductase component designated L-protein (a BchL dimer) and a catalytic component named NB-protein (a BchN-BchB heterotetramer), structure analysis and comparison to the nitrogenase complex, overview
additional information
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each catalytic BchN-BchB unit contains one protochlorophyllide and one iron-sulfur NB-cluster coordinated uniquely by one aspartate and three cysteines. Unique aspartate ligation is not necessarily needed for the cluster assembly but is essential for the catalytic activity. Specific protochlorophyllide-binding accompanies the partial unwinding of an alpha-helix that belongs to the next catalytic BchN-BchB unit, unique trans-specific reduction mechanism in which the distorted C17-propionate of protochlorophyllide and an aspartate from BchB serve as proton donors for C18 and C17 of protochlorophyllide, respectively, overview
additional information
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DPOR consists of two components: a reductase component designated L-protein (a BchL dimer) and a catalytic component named NB-protein (a BchN-BchB heterotetramer), structure analysis and comparison to the nitrogenase complex, overview. The NB-cluster is unique because it is coordinated by three Cys residues from BchN (BchN-Cys26, BchN-Cys51, BchN-Cys112) and one Asp residue from BchB (BchB-Asp36)
additional information
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each catalytic BchN-BchB unit contains one protochlorophyllide and one iron-sulfur NB-cluster coordinated uniquely by one aspartate and three cysteines. Unique aspartate ligation is not necessarily needed for the cluster assembly but is essential for the catalytic activity. Specific protochlorophyllide-binding accompanies the partial unwinding of an alpha-helix that belongs to the next catalytic BchN-BchB unit, unique trans-specific reduction mechanism in which the distorted C17-propionate of protochlorophyllide and an aspartate from BchB serve as proton donors for C18 and C17 of protochlorophyllide, respectively, overview
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additional information
Thermosynechococcus vestitus
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model of the complete hetero-octameric DPOR and distance between cofactors, overview
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L-protein in the MgADP-bound form, X-ray diffraction structure determination at 1.6 A resolution
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L-protein of DPOR with Mg-ADP bound, microcapillary batch diffusion method, with 20-25% (w/v) PEG 3350 as the precipitating agent, with 200 mM magnesium formate (pH 7.7)
substrate-bound, ADP-aluminium fluoride-stabilized transition state complex between the DPOR components L2 and (NB)2, sitting drops by vapor diffusion, mixing of 0.001 ml of protein solution containing 7.5 mg/ml protein in 100 mM HEPES/NaOH, pH 7.5, 150 mM NaCl, 10 mM MgCl2, 50 mM NaF, and 2 mM AlCl3,with 0.001 ml of reservoir solution containing 0.1 M KCl, 0.1 M Tris, pH 8.5, and 3% wt/v PEG 6000, 17Ā°C, X-ray diffraction structure determination and analysis at 2.1 A resolution
catalytic component NB-protein, both in thePchlide-bound and Pchlide-free states, X-ray diffraction structure determination at 2.3 A and 2.8 A resolution, respectively
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hanging drop vapor diffusion method, the protochlorophyllide-bound form of NB-protein is crystallized using 200 mM sodium/potassium phosphate buffer (pH 5.0) containing 5 mM dithiothreitol and 10% (w/v) ethylene glycol at 4Ā°C, to which 16% (w/v) and 14% (w/v) PEG4K are added in aerobic and anaerobic conditions, respectively, as precipitants. Protochlorophyllide -free and selenomethionine-substituted recombinant NB-proteins are crystallized at 20Ā°C using 20% (w/v) PEG3350 containing 200 mM ammonium chloride and 5mM dithiothreitol. D36C and D36A variants are crystallized at 4Ā°C using 20% (w/v) PEG3350 containing 200 mM sodium chloride, 100 mM MOPS/NaOH (pH 7.0) and 5 mM dithiothreitol as a precipitant
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purified recombinant protochlorophyllide-bound and protochlorophyllide-free forms of NB-protein of DPOR, and purified recombinant selenomethionine-substituted protochlorophyllide-free forms of mutants D36A and D36C, hanging-drop vapour diffusion method., X-ray diffraction structure determination and analysis at 2.3-2.9 A resolution
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native and SeMet-labeled catalytic (ChlN/ChlB)2 complex, hanging drop vapor diffusion, 17Ā°C, mixing of 0.003 ml of 10 mg/ml protein in 100 mM HEPES-NaOH, pH 7.5, 150 mM NaCl, and 10 mM MgCl2, with 0.003 ml of reservoir solution consisting of 9.5% PEG 6000, 85 mM HEPES-NaOH, pH 7.1, 14.3% 2-methyl pentane-2,4-diol, and 15% glycerol as cryoprotectants or 10.5% PEG 6000, 85 mM HEPES-NaOH, pH7.5, 14.3% 2-methyl pentane-2,4-diol, and 15% glycerol as cryoprotectants for selenomethionine-labeled protein, 3-5 days,X-ray diffraction structure determination and analysis at 2.4-2.81 A resolution
Thermosynechococcus vestitus
-
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C51A
-
the mutation almost abolishes the activity of the enzyme (less than 5% compared to the wild type enzyme)
C51A
-
the mutation almost abolishes the activity of the enzyme (less than 5% compared to the wild type enzyme)
-
C95A
Thermosynechococcus vestitus
-
inactive protein, probably due to destabilization of the [4Fe-4S] cluster environment
C95S
Thermosynechococcus vestitus
-
inactive protein, probably due to destabilization of the [4Fe-4S] cluster environment
D36A
-
site-directed mutagenesis, mutation in BchB, mutant NB-cluster structure compered to the wild-type enzyme
D36A
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the mutant exhibits low activity (13% compared to the wild type enzyme)
D36A
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site-directed mutagenesis, the mutant subunit B forms a complex with subunit N, indicating that Asp36 is not necessary for complex formation, D36A retains only 13% of wild-type activity
D36C
-
catalytically inactive
D36C
-
site-directed mutagenesis, mutation in BchB, mutant NB-cluster structure compered to the wild-type enzyme
D36C
-
the mutation almost abolishes the activity of the enzyme (less than 5% compared to the wild type enzyme)
D36C
-
site-directed mutagenesis, the mutant subunit B forms a complex with subunit N, indicating that Asp36 is not necessary for complex formation, catalytically inactive mutant
D36S
-
site-directed mutagenesis, mutation in BchB, mutant NB-cluster structure compered to the wild-type enzyme
D36S
-
the mutation almost abolishes the activity of the enzyme (less than 5% compared to the wild type enzyme)
D36S
-
site-directed mutagenesis, the mutant subunit B forms a complex with subunit N, indicating that Asp36 is not necessary for complex formation, catalytically inactive mutant
D36A
-
site-directed mutagenesis, mutation in BchB, mutant NB-cluster structure compered to the wild-type enzyme
-
D36A
-
the mutant exhibits low activity (13% compared to the wild type enzyme)
-
additional information
-
the ternary DPOR enzyme holocomplex comprising subunits ChlN, ChlB, and ChlL is trapped as an octameric (ChlN/ChlB)2(ChlL2)2 complex after incubation with the nonhydrolyzable ATP analogues adenosine 5'-(gamma-thio)triphosphate, adenosine 5'-(beta,gamma-imido)triphosphate, or MgADP in combination with AlF4-, complex structure, overview. A mutant ChlL2 protein, with a deleted Leu153 in the switch II region also allows for the formation of a stable octameric complex
additional information
-
construction of a DELTAchlL strain
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Fujita, Y.; Bauer, C.E.
Reconstitution of light-independent protochlorophyllide reductase from purified bchl and BchN-BchB subunits. In vitro confirmation of nitrogenase-like features of a bacteriochlorophyll biosynthesis enzyme
J. Biol. Chem.
275
23583-23588
2000
Rhodobacter capsulatus
brenda
Nomata, J.; Swem, L.R.; Bauer, C.E.; Fujita, Y.
Overexpression and characterization of dark-operative protochlorophyllide reductase from Rhodobacter capsulatus
Biochim. Biophys. Acta
1708
229-237
2005
Rhodobacter capsulatus
brenda
Shi, C.; Shi, X.
Characterization of three genes encoding the subunits of light-independent protochlorophyllide reductase in Chlorella protothecoides CS-41
Biotechnol. Prog.
22
1050-1055
2006
Auxenochlorella protothecoides (Q6VQA8 and Q6VQA9 and Q7YKW4), Auxenochlorella protothecoides
brenda
Nomata, J.; Ogawa, T.; Kitashima, M.; Inoue, K.; Fujita, Y.
NB-protein (BchN-BchB) of dark-operative protochlorophyllide reductase is the catalytic component containing oxygen-tolerant Fe-S clusters
FEBS Lett.
582
1346-1350
2008
Rhodobacter capsulatus
brenda
Shui, J.; Saunders, E.; Needleman, R.; Nappi, M.; Cooper, J.; Hall, L.; Kehoe, D.; Stowe-Evans, E.
Light-dependent and light-independent protochlorophyllide oxidoreductases in the chromatically adapting cyanobacterium Fremyella diplosiphon UTEX 481
Plant Cell Physiol.
50
1507-1521
2009
Microchaete diplosiphon (C6KHP5), Microchaete diplosiphon (Q6H056), Microchaete diplosiphon (Q6H058), Microchaete diplosiphon
brenda
Sarma, R.; Barney, B.M.; Hamilton, T.L.; Jones, A.; Seefeldt, L.C.; Peters, J.W.
Crystal structure of the L protein of Rhodobacter sphaeroides light-independent protochlorophyllide reductase with MgADP bound: a homologue of the nitrogenase Fe protein
Biochemistry
47
13004-13015
2008
Cereibacter sphaeroides (Q9RFD6), Cereibacter sphaeroides
brenda
Kondo, T.; Nomata, J.; Fujita, Y.; Itoh, S.
EPR study of 1Asp-3Cys ligated 4Fe-4S iron-sulfur cluster in NB-protein (BchN-BchB)2 of a dark-operative protochlorophyllide reductase complex
FEBS Lett.
585
214-218
2011
Rhodobacter capsulatus
brenda
Burke, D.H.; Alberti, M.; Hearst, J.E.
bchFNBH bacteriochlorophyll synthesis genes of Rhodobacter capsulatus and identification of the third subunit of light-independent protochlorophyllide reductase in bacteria and plants
J. Bacteriol.
175
2414-2422
1993
Rhodobacter capsulatus (D5ANS3), Rhodobacter capsulatus (P26163), Rhodobacter capsulatus (P26164), Rhodobacter capsulatus, Rhodobacter capsulatus SB1003 (D5ANS3)
brenda
Broecker, M.J.; Schomburg, S.; Heinz, D.W.; Jahn, D.; Schubert, W.D.; Moser, J.
Crystal structure of the nitrogenase-like dark operative protochlorophyllide oxidoreductase catalytic complex (ChlN/ChlB)2
J. Biol. Chem.
285
27336-27345
2010
Thermosynechococcus vestitus
brenda
Kusumi, J.; Sato, A.; Tachida, H.
Proceedings of the SMBE Tri-National Young Investigators Workshop 2005. Relaxation of functional constraint on light-independent protochlorophyllide oxidoreductase in Thuja
Mol. Biol. Evol.
23
941-948
2006
no activity in Thuja occidentalis, no activity in Thuja plicata, no activity in Thuja standishii, Cunninghamia lanceolata (Q2L604 and Q2L603 and Q2L602), Thujopsis dolabrata (Q2L614), Thujopsis dolabrata (Q2L615), Thujopsis dolabrata (Q2L616), Platycladus orientalis (Q2L619 and Q2L618 and Q2L617), Juniperus chinensis (Q2L622 and Q2L621 and Q2L620), Juniperus rigida (Q2L625 and Q2L624 and Q2L623), Cupressus sempervirens (Q2L628 and Q2L627 and Q2L626), Chamaecyparis lawsoniana (Q2L631 and Q2L630 and Q2L629), Chamaecyparis obtusa (Q2L634 and Q2L633 and Q2L632), Chamaecyparis pisifera (Q2L637 and Q2L636 and Q2L635), Taxodium distichum (Q2L640 and Q2L639 and Q2L638), Glyptostrobus pensilis (Q2L643 and Q2L642 and Q2L641), Cryptomeria japonica (Q2L646 and Q2L645 and Q2L644), Sequoiadendron giganteum (Q2L652 and Q2L651 and Q2L650), Sequoia sempervirens (Q2L655 and Q2L654 and Q2L653), Metasequoia glyptostroboides (Q2L658 and Q2L657 and Q2L656)
brenda
Muraki, N.; Nomata, J.; Ebata, K.; Mizoguchi, T.; Shiba, T.; Tamiaki, H.; Kurisu, G.; Fujita, Y.
X-ray crystal structure of the light-independent protochlorophyllide reductase
Nature
465
110-114
2010
Rhodobacter capsulatus, Rhodobacter capsulatus DB176
brenda
Fujita, Y.; Takagi, H.; Hase, T.
Identification of the chlB gene and the gene product essential for the light-independent chlorophyll biosynthesis in the cyanobacterium Plectonema boryanum
Plant Cell Physiol.
37
313-323
1996
Leptolyngbya boryana
brenda
Fujita, Y.; Takagi, H.; Hase, T.
Cloning of the gene encoding a protochlorophyllide reductase: the physiological significance of the co-existence of light-dependent and -independent protochlorophyllide reduction systems in the cyanobacterium Plectonema boryanum
Plant Cell Physiol.
39
177-185
1998
Leptolyngbya boryana
brenda
Skinner, J.S.; Timko, M.P.
Differential expression of genes encoding the light-dependent and light-independent enzymes for protochlorophyllide reduction during development in loblolly pine
Plant Mol. Biol.
39
577-592
1999
Pinus taeda
brenda
Raskin, V.I.; Schwartz, A.
Experimental approach to elucidating the mechanism of light-independent chlorophyll biosynthesis in greening barley
Plant Physiol.
133
25-28
2003
no activity in Hordeum vulgare
brenda
Broecker, M.J.; Waetzlich, D.; Saggu, M.; Lendzian, F.; Moser, J.; Jahn, D.
Biosynthesis of (bacterio)chlorophylls: ATP-dependent transient subunit interaction and electron transfer of dark operative protochlorophyllide oxidoreductase
J. Biol. Chem.
285
8268-8277
2010
Prochlorococcus marinus
brenda
Moser, J.; Broecker, M.J.
Methods for nitrogenase-like dark operative protochlorophyllide oxidoreductase
Methods Mol. Biol.
766
129-143
2011
Prochlorococcus marinus
brenda
Nazir, S.; Khan, M.S.
Chloroplast-encoded chlB gene from Pinus thunbergii promotes root and early chlorophyll pigment development in Nicotiana tabaccum
Mol. Biol. Rep.
39
10637-10646
2012
Pinus thunbergii
brenda
Breznenova”, K.; Demko, V.; Pavlovic, A.; Galova”, E.; Balazova”, R.; Hudak, J.
Light-independent accumulation of essential chlorophyll biosynthesis- and photosynthesis-related proteins in Pinus mugo and Pinus sylvestris seedlings
Photosynthetica
48
16-22
2010
Pinus mugo (C7EP38), Pinus sylvestris (G8ITI1)
-
brenda
Kopecna, J.; Sobotka, R.; Komenda, J.
Inhibition of chlorophyll biosynthesis at the protochlorophyllide reduction step results in the parallel depletion of photosystem I and photosystem II in the cyanobacterium Synechocystis PCC 6803
Planta
237
497-508
2013
Synechocystis sp.
brenda
Moser, J.; Lange, C.; Krausze, J.; Rebelein, J.; Schubert, W.D.; Ribbe, M.W.; Heinz, D.W.; Jahn, D.
Structure of ADP-aluminium fluoride-stabilized protochlorophyllide oxidoreductase complex
Proc. Natl. Acad. Sci. USA
110
2094-2098
2013
Prochlorococcus marinus (Q7VD39), Prochlorococcus marinus
brenda
Reinbothe, C.; El Bakkouri, M.; Buhr, F.; Muraki, N.; Nomata, J.; Kurisu, G.; Fujita, Y.; Reinbothe, S.
Chlorophyll biosynthesis: spotlight on protochlorophyllide reduction
Trends Plant Sci.
15
614-624
2010
Chlorobaculum tepidum, Chloroflexus aurantiacus, Prochlorococcus marinus, Rhodobacter capsulatus, Cereibacter sphaeroides, Heliobacterium mobile
brenda
Nomata, J.; Terauchi, K.; Fujita, Y.
Stoichiometry of ATP hydrolysis and chlorophyllide formation of dark-operative protochlorophyllide oxidoreductase from Rhodobacter capsulatus
Biochem. Biophys. Res. Commun.
470
704-709
2016
Rhodobacter capsulatus (D5ANS3 and P26164 and P26163), Rhodobacter capsulatus ATCC BAA-309 (D5ANS3 and P26164 and P26163)
brenda
Zhang, D.; Li, Y.; Zhang, X.; Zha, P.; Lin, R.
The SWI2/SNF2 chromatin-remodeling ATPase BRAHMA regulates chlorophyll biosynthesis in Arabidopsis
Mol. Plant
10
155-167
2017
Arabidopsis thaliana (Q42536)
brenda
Silva, P.J.
With or without light comparing the reaction mechanism of dark-operative protochlorophyllide oxidoreductase with the energetic requirements of the light-dependent protochlorophyllide oxidoreductase
PeerJ
2
e551
2014
Rhodobacter capsulatus (P26164), Rhodobacter capsulatus ATCC BAA-309 (P26164)
brenda