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heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
heme + electron donor + O2
alpha-biliverdin + beta-biliverdin + delta-biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
-
wild-type, mutant N19K, mutant F117Y, 30% beta- and 70% delta-isomer, N19K/F117Y double mutant, 55% alpha-, 10% beta-, 35% delta-isoform
-
?
heme + electron donor + O2
biliverdin IXalpha + Fe2+ + CO + oxidized eletron donor + H2O
-
prefers ferredoxin or ascorbate as electron donor
-
-
?
protoheme + reduced acceptor + O2
biliverdin-IX-beta + CO + Fe2+ + acceptor + H2O
-
-
-
-
?
protoheme + reduced acceptor + O2
biliverdin-IX-delta + CO + Fe2+ + acceptor + H2O
-
-
-
-
?
additional information
?
-
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
natural electron donor for PigA from Pseudomonas aeruginosa PAO1 is ferredoxin-NADP+-oxidoreductase
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
with NADPH, ascorbate, FNR and ferredoxin as exogenous reductant system, spectroscopic determination
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
with NADPH, ferredoxin from spinach, and spinach ferredoxin-NADP+-oxidoreductase
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
with NADPH, ascorbate, FNR and ferredoxin as exogenous reductant system, spectroscopic determination
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
with NADPH, ascorbate, FNR and ferredoxin as exogenous reductant system, spectroscopic determination
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
with NADPH, ascorbate, FNR and ferredoxin as exogenous reductant system, spectroscopic determination
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
with NADPH, ascorbate, FNR and ferredoxin as exogenous reductant system, spectroscopic determination
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
with NADPH, ascorbate, FNR and ferredoxin as exogenous reductant system, spectroscopic determination
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
with NADPH, ascorbate, FNR and ferredoxin as exogenous reductant system, spectroscopic determination
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
with NADPH, ascorbate, FNR and ferredoxin as exogenous reductant system, spectroscopic determination
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
with NADPH, ascorbate, FNR and ferredoxin as exogenous reductant system, spectroscopic determination
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
with NADPH, ascorbate, FNR and ferredoxin as exogenous reductant system, spectroscopic determination
-
-
?
additional information
?
-
-
BphO, a heme oxygenase, produces the linear tetrapyrrole chromophore biliverdin IXa, potential protective role of the BphO reaction product biliverdin, overview
-
-
?
additional information
?
-
the organism contains only one enzyme type: PigA. PigA produces the biliverdin isomer IXalpha
-
-
?
additional information
?
-
the organism contains only one enzyme type: PigA. PigA produces the biliverdin isomer IXalpha
-
-
?
additional information
?
-
the organism contains only one enzyme type: PigA. PigA produces the biliverdin isomer IXalpha
-
-
?
additional information
?
-
the organism contains two heme oxygenases with different regiospecificities: BphO and PigA. While BphO cleaves heme to exclusively yield biliverdin IXalpha, PigA produces the biliverdin isomers IXbeta and IXdelta
-
-
?
additional information
?
-
the organism contains two heme oxygenases with different regiospecificities: BphO and PigA. While BphO cleaves heme to exclusively yield biliverdin IXalpha, PigA produces the biliverdin isomers IXbeta and IXdelta
-
-
?
additional information
?
-
the organism contains two heme oxygenases with different regiospecificities: BphO and PigA. While BphO cleaves heme to exclusively yield biliverdin IXalpha, PigA produces the biliverdin isomers IXbeta and IXdelta
-
-
?
additional information
?
-
the organism contains only one enzyme type: PigA. PigA produces the biliverdin isomer IXalpha
-
-
?
additional information
?
-
the organism contains two heme oxygenases with different regiospecificities: BphO and PigA. While BphO cleaves heme to exclusively yield biliverdin IXalpha, PigA produces the biliverdin isomers IXbeta and IXdelta
-
-
?
additional information
?
-
the organism contains two heme oxygenases with different regiospecificities: BphO and PigA. While BphO cleaves heme to exclusively yield biliverdin IXalpha, PigA produces the biliverdin isomers IXbeta and IXdelta
-
-
?
additional information
?
-
the organism contains two heme oxygenases with different regiospecificities: BphO and PigA. While BphO cleaves heme to exclusively yield biliverdin IXalpha, PigA produces the biliverdin isomers IXbeta and IXdelta
-
-
?
additional information
?
-
the organism contains two heme oxygenases with different regiospecificities: BphO and PigA. While BphO cleaves heme to exclusively yield biliverdin IXalpha, PigA produces the biliverdin isomers IXbeta and IXdelta
-
-
?
additional information
?
-
the organism contains two heme oxygenases with different regiospecificities: BphO and PigA. While BphO cleaves heme to exclusively yield biliverdin IXalpha, PigA produces the biliverdin isomers IXbeta and IXdelta
-
-
?
additional information
?
-
the organism contains two heme oxygenases with different regiospecificities: BphO and PigA. While BphO cleaves heme to exclusively yield biliverdin IXalpha, PigA produces the biliverdin isomers IXbeta and IXdelta
-
-
?
additional information
?
-
the organism contains only one enzyme type: PigA. PigA produces the biliverdin isomer IXalpha
-
-
?
additional information
?
-
the organism contains only one enzyme type: PigA. PigA produces the biliverdin isomer IXalpha
-
-
?
additional information
?
-
the organism contains two heme oxygenases with different regiospecificities: BphO and PigA. While BphO cleaves heme to exclusively yield biliverdin IXalpha, PigA produces the biliverdin isomers IXbeta and IXdelta
-
-
?
additional information
?
-
the organism contains two heme oxygenases with different regiospecificities: BphO and PigA. While BphO cleaves heme to exclusively yield biliverdin IXalpha, PigA produces the biliverdin isomers IXbeta and IXdelta
-
-
?
additional information
?
-
the organism contains two heme oxygenases with different regiospecificities: BphO and PigA. While BphO cleaves heme to exclusively yield biliverdin IXalpha, PigA produces the biliverdin isomers IXbeta and IXdelta
-
-
?
additional information
?
-
the organism contains two heme oxygenases with different regiospecificities: BphO and PigA. While BphO cleaves heme to exclusively yield biliverdin IXalpha, PigA produces the biliverdin isomers IXbeta and IXdelta
-
-
?
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heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
protoheme + reduced acceptor + O2
biliverdin-IX-beta + CO + Fe2+ + acceptor + H2O
-
-
-
-
?
protoheme + reduced acceptor + O2
biliverdin-IX-delta + CO + Fe2+ + acceptor + H2O
-
-
-
-
?
additional information
?
-
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
natural electron donor for PigA from Pseudomonas aeruginosa PAO1 is ferredoxin-NADP+-oxidoreductase
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
-
-
?
additional information
?
-
-
BphO, a heme oxygenase, produces the linear tetrapyrrole chromophore biliverdin IXa, potential protective role of the BphO reaction product biliverdin, overview
-
-
?
additional information
?
-
the organism contains only one enzyme type: PigA. PigA produces the biliverdin isomer IXalpha
-
-
?
additional information
?
-
the organism contains only one enzyme type: PigA. PigA produces the biliverdin isomer IXalpha
-
-
?
additional information
?
-
the organism contains only one enzyme type: PigA. PigA produces the biliverdin isomer IXalpha
-
-
?
additional information
?
-
the organism contains only one enzyme type: PigA. PigA produces the biliverdin isomer IXalpha
-
-
?
additional information
?
-
the organism contains two heme oxygenases with different regiospecificities: BphO and PigA. While BphO cleaves heme to exclusively yield biliverdin IXalpha, PigA produces the biliverdin isomers IXbeta and IXdelta
-
-
?
additional information
?
-
the organism contains two heme oxygenases with different regiospecificities: BphO and PigA. While BphO cleaves heme to exclusively yield biliverdin IXalpha, PigA produces the biliverdin isomers IXbeta and IXdelta
-
-
?
additional information
?
-
the organism contains two heme oxygenases with different regiospecificities: BphO and PigA. While BphO cleaves heme to exclusively yield biliverdin IXalpha, PigA produces the biliverdin isomers IXbeta and IXdelta
-
-
?
additional information
?
-
the organism contains two heme oxygenases with different regiospecificities: BphO and PigA. While BphO cleaves heme to exclusively yield biliverdin IXalpha, PigA produces the biliverdin isomers IXbeta and IXdelta
-
-
?
additional information
?
-
the organism contains two heme oxygenases with different regiospecificities: BphO and PigA. While BphO cleaves heme to exclusively yield biliverdin IXalpha, PigA produces the biliverdin isomers IXbeta and IXdelta
-
-
?
additional information
?
-
the organism contains two heme oxygenases with different regiospecificities: BphO and PigA. While BphO cleaves heme to exclusively yield biliverdin IXalpha, PigA produces the biliverdin isomers IXbeta and IXdelta
-
-
?
additional information
?
-
the organism contains only one enzyme type: PigA. PigA produces the biliverdin isomer IXalpha
-
-
?
additional information
?
-
the organism contains only one enzyme type: PigA. PigA produces the biliverdin isomer IXalpha
-
-
?
additional information
?
-
the organism contains two heme oxygenases with different regiospecificities: BphO and PigA. While BphO cleaves heme to exclusively yield biliverdin IXalpha, PigA produces the biliverdin isomers IXbeta and IXdelta
-
-
?
additional information
?
-
the organism contains two heme oxygenases with different regiospecificities: BphO and PigA. While BphO cleaves heme to exclusively yield biliverdin IXalpha, PigA produces the biliverdin isomers IXbeta and IXdelta
-
-
?
additional information
?
-
the organism contains two heme oxygenases with different regiospecificities: BphO and PigA. While BphO cleaves heme to exclusively yield biliverdin IXalpha, PigA produces the biliverdin isomers IXbeta and IXdelta
-
-
?
additional information
?
-
the organism contains two heme oxygenases with different regiospecificities: BphO and PigA. While BphO cleaves heme to exclusively yield biliverdin IXalpha, PigA produces the biliverdin isomers IXbeta and IXdelta
-
-
?
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(2E)-2-[4-(dimethylamino)benzylidene]hydrazinecarboximidamide
-
binding affinity 0.030 mM
(2E)-2-[[4-(dimethylamino)phenyl]methylidene]hydrazinecarboximidamide
-
binding affinity is 0.030 mM, complete inhibition
(2Z)-4-[(4-anilinophenyl)amino]-4-oxobut-2-enoic acid
-
binding affinity 0.0201 mM, above 0.25 mM significant decrease in growth of strain on heme as sole source of iron
(2Z)-N'-[(1Z)-pyridin-3-ylmethylene]-2-(pyridin-3-ylmethylene)hydrazinecarboximidohydrazide
-
binding affinity 0.0159 mM
(2Z)-N'-[(1Z)-pyridin-3-ylmethylidene]-2-(pyridin-3-ylmethylidene)hydrazinecarboximidohydrazide
-
binding affinity is 0.0159 mM, complete inhibition
1-(2,4-dinitrophenyl)methanamine
-
binding affinity 0.187 mM
2-(4-chlorophenyl)-N'-[(1E)-1H-indol-3-ylmethylidene]acetohydrazide
-
binding affinity is 0.0158 mM, complete inhibition
2-(4-chlorophenyl)-N'-[(1Z)-1H-inden-3-ylmethylene]acetohydrazide
-
binding affinity 0.0158 mM, above 0.25 mM significant decrease in growth of strain on heme as sole source of iron
4-oxo-4-[[4-(phenylamino)phenyl]amino]butanoic acid
-
binding affinity is 0.0201 mM, complete inhibition
4-[(2-hydroxyphenyl)amino]naphthalene-1,2-dione
-
binding affinity is 0.0728 mM, partial inhibition
N'-(pyridin-4-ylcarbonyl)pyridine-4-carbohydrazide
-
binding affinity is 0.0447 mM, partial inhibition
N-(4-imidazo[1,2-a]pyridin-2-ylphenyl)-2-nitrobenzamide
-
binding affinity is 0.0061 mM, complete inhibition
N-(4-imidazo[1,2-a]pyridin-2-ylphenyl)-3-nitrobenzamide
-
binding affinity 0.0061 mM
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F117Y
-
no change in regioselectivity
F189A
-
the heme degradation activity of the mutant is similar to that of the wild-type enzyme. The mutant produces only beta- and delta-biliverdins, but no alpha-biliverdin
F189G
-
the heme degradation activity of the mutant is similar to that of the wild-type enzyme. The mutant produces only beta- and delta-biliverdins, but no alpha-biliverdin
F189L
-
the heme degradation activity of the mutant is similar to that of the wild-type enzyme. The mutant produces only beta- and delta-biliverdins, but no alpha-biliverdin
F189T
-
the heme degradation activity of the mutant is similar to that of the wild-type enzyme. The mutant produces only beta- and delta-biliverdins, but no alpha-biliverdin
G125V
-
single-phase kinetics of transfer of heme from heme-binding protein PhuS
H26A/K34A/K132A
-
inactive
K132A
-
the heme degradation activity of the mutant is similar to that of the wild-type enzyme, but the mutant produces 12% of alpha-biliverdin in addition to the formation of normal beta- (26%) and delta- (62%) biliverdins
K34A
-
the heme degradation activity of the mutant is similar to that of the wild-type enzyme, but the mutant produces 11% of alpha-biliverdin in addition to the formation of normal beta- (34%) and delta- (55%) biliverdins
K34A/K132A
-
the heme degradation activity of the mutant is similar to that of the wild-type enzyme, but the mutant produces 18% of alpha-biliverdin in addition to the formation of normal beta- (27%) and delta- (56%) biliverdins
N19K
-
no change in regioselectivity
N19K/F117Y/K132A
-
destabilization of heme within the protein, transfer of heme from heme binding protein PhuS is not affected and shows biphasic kinetics
N19K/F117Y/K34N
-
destabilization of heme within the protein, transfer of heme from heme binding protein PhuS is not affected and shows biphasic kinetics
N19K/K34A/F117Y/K132A
-
the mutant produces biliverdin-IX-alpha
R80L
-
mutant exhibits allmost global conformational disorder related to significantly lower efficiency to hydroxylate heme in the presence of H2O2
T189W
-
the heme degradation activity of the mutant is similar to that of the wild-type enzyme. The mutant produces only beta- and delta-biliverdins, but no alpha-biliverdin
additional information
-
chromosomal knock-out gene bphO mutants shows identical growth behavior as the wild type under various conditions, the bphO mutant and the double mutant strain DELTAbphO show increased levels of pyocyanin, as well as decreased heat tolerance in the stationary phase, phenotypes, overview
N19K/F117Y
-
change in regioselectivity, producing alpha-biliverdin and less beta- and delta-biliverdin, enzyme exists as a mixture of molecules exhibiting 2 distinct heme seatings, one seating is identical to wild-type, the other is similar to that typical of alpha-hydroxylating heme oxigenases
N19K/F117Y
-
destabilization of heme within the protein, transfer of heme from heme binding protein PhuS is not affected and shows biphasic kinetics
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expressed in a Neisseria meningitidis HemO deletion mutant
-
expressed in Escherichia coli BL21(DE3) cells
-
gene bphO, BphO is genetically coupled to the phytochrome BphP, expression of GST-tagged BphO in Escherichia coli strain BL21(DE3)
gene bphO, BphO is genetically coupled to the phytochrome BphP, expression of N-terminally His6-tagged BphO in Escherichia coli strain BL21(DE3)
gene bphOP, DNA and amino acid sequence, including promoter, determination and analysis, expression analysis, dependence of bphOP expression on RpoS
-
gene pigA, pigA genes are organized in gene clusters associated with iron utilization, expression of GST-tagged PigA in Escherichia coli strain BL21(DE3)
genes pigA, two homologues, one of the two PigA homologues identified in Pseudomonas putida KT2440 is encoded in an iron-associated gene cluster, expression of GST-tagged PigA and BphO in Escherichia coli strain BL21(DE3)
gene bphO, BphO is genetically coupled to the phytochrome BphP, expression of GST-tagged BphO in Escherichia coli strain BL21(DE3)
gene bphO, BphO is genetically coupled to the phytochrome BphP, expression of GST-tagged BphO in Escherichia coli strain BL21(DE3)
gene bphO, BphO is genetically coupled to the phytochrome BphP, expression of GST-tagged BphO in Escherichia coli strain BL21(DE3)
gene pigA, pigA genes are organized in gene clusters associated with iron utilization, expression of GST-tagged PigA in Escherichia coli strain BL21(DE3)
gene pigA, pigA genes are organized in gene clusters associated with iron utilization, expression of GST-tagged PigA in Escherichia coli strain BL21(DE3)
gene pigA, pigA genes are organized in gene clusters associated with iron utilization, expression of GST-tagged PigA in Escherichia coli strain BL21(DE3)
gene pigA, pigA genes are organized in gene clusters associated with iron utilization, expression of GST-tagged PigA in Escherichia coli strain BL21(DE3)
genes pigA, two homologues, one of the two PigA homologues identified in Pseudomonas putida KT2440 is encoded in an iron-associated gene cluster, expression of GST-tagged PigA and BphO in Escherichia coli strain BL21(DE3)
genes pigA, two homologues, one of the two PigA homologues identified in Pseudomonas putida KT2440 is encoded in an iron-associated gene cluster, expression of GST-tagged PigA and BphO in Escherichia coli strain BL21(DE3)
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Wegele, R.; Tasler, R.; Zeng, Y.; Rivera, M.; Frankenberg-Dinkel, N.
The heme oxygenase(s)-phytochrome system of Pseudomonas aeruginosa
J. Biol. Chem.
279
45791-45802
2004
Pseudomonas aeruginosa
brenda
Caignan, G.A.; Deshmukh, R.; Wilks, A.; Zeng, Y.; Huang, H.W.; Moenne-Loccoz, P.; Bunce, R.A.; Eastman, M.A.; Rivera, M.
Oxidation of heme to beta- and delta-biliverdin by Pseudomonas aeruginosa heme oxygenase as a consequence of an unusual seating of the heme
J. Am. Chem. Soc.
124
14879-14892
2002
Pseudomonas aeruginosa
brenda
Bhakta, M.N.; Wilks, A.
The mechanism of heme transfer from the cytoplasmic heme binding protein PhuS to the delta-regioselective heme oxygenase of Pseudomonas aeruginosa
Biochemistry
45
11642-11649
2006
Pseudomonas aeruginosa
brenda
Rodrguez, J.C.; Wilks, A.; Rivera, M.
Backbone NMR assignments and H/D exchange studies on the ferric azide- and cyanide-inhibited forms of Pseudomonas aeruginosa heme oxygenase
Biochemistry
45
4578-4592
2006
Pseudomonas aeruginosa
brenda
Rodrguez, J.C.; Zeng, Y.; Wilks, A.; Rivera, M.
The hydrogen-bonding network in heme oxygenase also functions as a modulator of enzyme dynamics: chaotic motions upon disrupting the H-bond network in heme oxygenase from Pseudomonas aeruginosa
J. Am. Chem. Soc.
129
11730-11742
2007
Pseudomonas aeruginosa
brenda
Furci, L.M.; Lopes, P.; Eakanunkul, S.; Zhong, S.; MacKerell, A.D.; Wilks, A.
Inhibition of the bacterial heme oxygenases from Pseudomonas aeruginosa and Neisseria meningitidis: novel antimicrobial targets
J. Med. Chem.
50
3804-3813
2007
Pseudomonas aeruginosa
brenda
Barkovits, K.; Harms, A.; Benkartek, C.; Smart, J.L.; Frankenberg-Dinkel, N.
Expression of the phytochrome operon in Pseudomonas aeruginosa is dependent on the alternative sigma factor RpoS
FEMS Microbiol. Lett.
80
160-168
2008
Pseudomonas aeruginosa
brenda
Gisk, B.; Wiethaus, J.; Aras, M.; Frankenberg-Dinkel, N.
Variable composition of heme oxygenases with different regiospecificities in Pseudomonas species
Arch. Microbiol.
194
597-606
2012
Pseudomonas mendocina (A4Y0Y8), Pseudomonas aeruginosa (O69002), Pseudomonas aeruginosa (Q88P48), Pseudomonas aeruginosa (Q9HWR4), Pseudomonas fluorescens (Q4K657), Pseudomonas fluorescens (Q4K7S1), Pseudomonas syringae pv. tomato (Q885D4), Pseudomonas syringae pv. tomato (Q887K9), Pseudomonas putida (Q88JR7), Pseudomonas fluorescens Pf-5 (Q4K657), Pseudomonas fluorescens Pf-5 (Q4K7S1), Pseudomonas syringae pv. tomato DC3000 (Q885D4), Pseudomonas syringae pv. tomato DC3000 (Q887K9), Pseudomonas aeruginosa KT 2240 (Q88P48), Pseudomonas putida KT 2240 (Q88JR7), Pseudomonas mendocina YMP (A4Y0Y8)
brenda
Fujii, H.; Zhang, X.; Yoshida, T.
Essential amino acid residues controlling the unique regioselectivity of heme oxygenase in Pseudomonas aeruginosa
J. Am. Chem. Soc.
126
4466-4467
2004
Pseudomonas aeruginosa
brenda
Ratliff, M.; Zhu, W.; Deshmukh, R.; Wilks, A.; Stojiljkovic, I.
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