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protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
mechanism
-
protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
a ferric hydroperoxide species must be an active intermediate in the first oxygenation step
-
protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
determination of single turnover rate constants and reaction intermediates for heme oxygenase-1
-
protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
hydroperoxoferri-heme oxygenase-1 is the reactive species directly forming the alpha-meso-hydroxyheme product by attack of the distal OH of the hydroperoxo moiety at the heme alpha-carbon
-
protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
binding of heme stabilizes the solvent H-bonded network in the active site required for proper catalysis
-
protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
docking model of heme and ferredoxin, indirect electron transfer from an iron-sulfur cluster in ferredoxin to the heme iron
-
protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
electrophilic oxidation mechanism, stereochemical control of the reaction regiospecificity
protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
model of activation mechanism of Fe-OOH
protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
model of active site
protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
opened conformation of the heme pocket facilitates sequential product release, first iron, then biliverdin, iron triggers slow dissociation of biliverdin
protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
rate-limiting step of reaction is biliverdin release
-
protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
selective oxygenation at the alpha-meso carbon, model of active site
protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
a three-step mechanism, mechanism of the the third step, heme oxygenase enzymatic ring-opening mechanism of verdoheme, a process which maintains iron homeostasis, overview. Reaction mechanism for the FeOOH pathway and the FeHOOH pathway, and complete triplet-state mechanism, overview
protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
heme degradation by heme oxygenase proceeds through three successive steps of O2 activation. The first step is formation of alpha-meso-hydroxyheme from from heme, second formation of verdoheme from alpha-meso-hydroxyheme, the third step is the ring opening of alpha-verdoheme to alpha-biliverdin, overview
-
protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
heme degradation by heme oxygenase proceeds through three successive steps of O2 activation. The first step is formation of alpha-meso-hydroxyheme from heme, second formation of verdoheme from alpha-meso-hydroxyheme, the third step is the ring opening of verdoheme. Only alpha-verdoheme with the O atom in its alpha position, and not beta-, gamma-, or delta-verdoheme, is converted to biliverdin. The third step, like the first, shows regiospecificity, the distal Asp plays an important role in this step, similar to the first. The substrate heme is sandwiched between two helices, termed the proximal and distal helices. Reaction mechanism, overview
protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
heme degradation by heme oxygenase proceeds through three successive steps of O2 activation. The first step is formation of alpha-meso-hydroxyheme from heme, second formation of verdoheme from alpha-meso-hydroxyheme, the third step is the ring opening of verdoheme. Only alpha-verdoheme with the O atom in its alpha position, and not beta-, gamma-, or delta-verdoheme, is converted to biliverdin. The third step, like the first, shows regiospecificity, the distal Asp plays an important role in this step, similar to the first. The substrate heme is sandwiched between two helices, termed the proximal and distal helices. Reaction mechanism, overview
protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
heme degradation by heme oxygenase proceeds through three successive steps of O2 activation. The first step is formation of alpha-meso-hydroxyheme from heme, second formation of verdoheme from alpha-meso-hydroxyheme, the third step is the ring opening of verdoheme. Only alpha-verdoheme with the O atom in its alpha position, and not beta-, gamma-, or delta-verdoheme, is converted to biliverdin. The third step, like the first, shows regiospecificity, the distal Asp plays an important role in this step, similar to the first. The substrate heme is sandwiched between two helices, termed the proximal and distal helices. Reaction mechanism, overview
protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
-
-
-
-
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15-phenylheme + electron donor + O2
10-phenylbiliverdin IXalpha + Fe2+ + CO + oxidized eletron donor + H2O
-
-
-
?
5-phenylheme + electron donor + O2
biliverdin IXalpha + Fe2+ + CO + oxidized eletron donor + H2O + benzoic acid
-
-
-
?
alpha-meso-formylmesoheme + NADPH
? + NADP+
-
exclusively oxidized at a non-formyl substituted meso-carbon
-
?
alpha-meso-hydroxyhemin IX + reduced acceptor + O2
verdoheme IXalpha + CO + acceptor + H2O
-
-
-
-
?
alpha-meso-oxyprotoheme IX + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
r
beta-meso-hydroxyhemin IX + reduced acceptor + O2
verdoheme IXbeta + CO + acceptor + H2O
-
-
-
-
?
Co-heme + NADPH + H+ + O2
biliverdin Ixalpha + Co2+ + CO + NAD+ + H2O
-
-
-
-
r
delta-meso-hydroxyhemin IX + reduced acceptor + O2
verdoheme IXdelta + CO + acceptor + H2O
-
-
-
-
?
Fe-heme + [reduced NADPH-hemoprotein reductase] + O2
biliverdin Ixalpha + Fe2+ + CO + NAD+ + H2O
-
-
-
-
r
gamma-CH-Fe(cor) + 3 AH2 + 3 O2
?
gamma-meso-hydroxyhemin IX + reduced acceptor + O2
verdoheme IXgamma + CO + acceptor + H2O
-
-
-
-
?
hematoheme + NADPH + H+ + O2
hematobiliverdin Fe2+ + CO + NAD+ + H2O
-
-
-
-
r
heme + 2 NADH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NAD+ + H2O
-
NADH-dependent heme degradation system may have a biological role in regulating the concentration of respiratory hemoproteins and the disposition of the aberrant forms of the mitochondrial hemoproteins
-
?
heme + 2 NADPH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NADP+ + H2O
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
heme + 3 AH2 + 3 O2
biliverdin IXalpha + Fe2+ + CO + 3 A + 3 H2O
heme + 3 reduced ascorbate + 3 O2
biliverdin + Fe2+ + CO + 3 oxidized ascorbate + 3 H2O
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized electron donor + H2O
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
heme + ferredoxin + O2
biliverdin IXalpha + Fe2+ + CO + A + H2O
-
HY1, HO3, and HO4
-
-
?
heme + NADH + O2
biliverdin + Fe2+ + CO + NAD+ + H2O
heme + NADPH + H+ + O2
biliverdin IXalpha + Fe2+ + CO + NADP+ + H2O
heme + NADPH + H+ + O2
biliverdin IXdelta + biliverdin IXalpha + Fe2+ + CO + NADP+ + H2O
-
mutant R183E, yields about 20% of product biliverdin IXdelta
-
?
heme + [reduced NADPH-hemoprotein reductase] + O2
biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
heme c + NADPH + H+ + O2
biliverdin c + Fe2+ + CO + NAD+ + H2O
-
-
-
-
r
hemin + reduced acceptor + O2
alpha-meso-hydroxyhemin IX + CO + acceptor + H2O
-
-
-
-
?
methemoglobin + electron donor + O2
?
protoheme + reduced acceptor + O2 + Fe2+
biliverdin-IX-alpha + CO + Fe3+ + acceptor + H2O
-
-
-
-
?
protoheme + [reduced cytochrome P450 reductase] + O2
biliverdin + Fe2+ + CO + [oxidized cytochrome P450 reductase] + H2O
-
-
-
?
protoheme + [reduced NADPH-hemoprotein reductase] + H+ + O2
biliverdin-IX-alpha + CO + Fe2+ + [oxidized NADPH-hemoprotein reductase] + H2O
protoheme + [reduced NADPH-hemoprotein reductase] + O2
biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
protoheme + [reduced NADPH-hemoprotein reductase] + O2
biliverdin IXbeta + biliverdin IXdelta + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
verdoheme IXalpha + H2O
biliverdin IXalpha + Fe2+
-
-
-
-
?
additional information
?
-
gamma-CH-Fe(cor) + 3 AH2 + 3 O2
?
-
the regioisomeric iron corrole is an artificial, not-natural substrate, the enzymatic cleavage happens selectively at the unexpected bipyrrolic position and yields a biomimetic biliverdin-like product. The enzymatic corrole ring opening is selective for this corrole regioisomer and for plant-type heme oxygenase, mechanism, overview
-
-
?
gamma-CH-Fe(cor) + 3 AH2 + 3 O2
?
-
the regioisomeric iron corrole is an artificial, not-natural substrate, the enzymatic cleavage happens selectively at the unexpected bipyrrolic position and yields a biomimetic biliverdin-like product. The enzymatic corrole ring opening is selective for this corrole regioisomer and for plant-type heme oxygenase, mechanism, overview
-
-
?
heme + 2 NADPH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NADP+ + H2O
-
-
-
-
?
heme + 2 NADPH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NADP+ + H2O
-
involved in heme metabolism
-
?
heme + 2 NADPH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NADP+ + H2O
-
-
-
-
?
heme + 2 NADPH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NADP+ + H2O
-
involved in heme metabolism
-
?
heme + 2 NADPH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NADP+ + H2O
-
-
-
-
?
heme + 2 NADPH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NADP+ + H2O
-
-
-
?
heme + 2 NADPH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NADP+ + H2O
-
-
-
-
?
heme + 2 NADPH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NADP+ + H2O
-
involved in heme metabolism
-
?
heme + 2 NADPH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NADP+ + H2O
-
involved in heme metabolism
-
?
heme + 2 NADPH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NADP+ + H2O
-
-
-
-
?
heme + 2 NADPH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NADP+ + H2O
-
involved in heme metabolism
-
?
heme + 2 NADPH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NADP+ + H2O
-
involved in heme metabolism
-
?
heme + 2 NADPH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NADP+ + H2O
-
involved in heme metabolism
-
?
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
-
requires three oxidative reaction steps, via alpha-meso-hydroxy-heme and verdoheme, detailed overview
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
reaction intermediate verdoheme and the verdoheme-enzyme complex are gradually degraded in the presence of O2
-
-
?
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
-
requires three oxidative reaction steps, via alpha-meso-hydroxy-heme and verdoheme, detailed overview
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
reaction intermediate verdoheme and the verdoheme-enzyme complex are gradually degraded in the presence of O2
-
-
?
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
requires three oxidative reaction steps, via alpha-meso-hydroxy-heme and verdoheme, detailed overview
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
reaction intermediate verdoheme and the verdoheme-enzyme complex are gradually degraded in the presence of O2
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
-
-
?
heme + 3 AH2 + 3 O2
biliverdin IXalpha + Fe2+ + CO + 3 A + 3 H2O
-
-
-
?
heme + 3 AH2 + 3 O2
biliverdin IXalpha + Fe2+ + CO + 3 A + 3 H2O
-
-
-
-
?
heme + 3 reduced ascorbate + 3 O2
biliverdin + Fe2+ + CO + 3 oxidized ascorbate + 3 H2O
-
-
-
-
?
heme + 3 reduced ascorbate + 3 O2
biliverdin + Fe2+ + CO + 3 oxidized ascorbate + 3 H2O
-
-
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
-
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
-
-
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
HO-1 is a critical cell defence enzyme against oxidative stress, HO-1 participates in the protective effect afforded by neuronal nicotinic acetylcholine receptors, nAChR, activation, which activates the neuroprotective signaling cascade, overview
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
induction of HO-1 leads to a reduction of superoxide and increases levels of spermine-NoNoate, HO-1 is involved in artery vascular relaxation, overview
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
-
-
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
-
induction of HO-1 via the ERK-Nrf2-ARE signaling pathway is involved in protecting cells from oxidative stress, overview
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
-
-
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
-
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
-
-
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
-
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
-
-
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
-
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
-
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
-
-
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
-
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
-
-
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
-
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
-
-
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
-
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
-
-
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
-
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
activation of the enzyme leads to induction of the ABC transporter ABCG2, but not of ABCB6
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
biliverdin is involved in hemin degradation
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
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1.14.14.18 heme oxygenase (biliverdin-producing)
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