1.14.14.18: heme oxygenase (biliverdin-producing)
This is an abbreviated version!
For detailed information about heme oxygenase (biliverdin-producing), go to the full flat file.
Word Map on EC 1.14.14.18
-
1.14.14.18
-
monoxide
-
cytoprotective
-
endothelial
-
necrosis
-
dismutase
-
protoporphyrin
-
erythroid
-
2-related
-
tnf
-
bilirubin
-
artery
-
malondialdehyde
-
lipopolysaccharide
-
catalase
-
hemin
-
neuroprotective
-
ischemia
-
gsh
-
lps
-
sod
-
anti-oxidant
-
mapks
-
sirna
-
caspase-3
-
quinone
-
pulmonary
-
reperfusion
-
lps-induced
-
hypoxia
-
cyclooxygenase-2
-
cox-2
-
ferritin
-
erk
-
nf-e2-related
-
anti-apoptotic
-
cobalt
-
myeloperoxidase
-
ischemia-reperfusion
-
nrf2-mediated
-
pro-oxidant
-
kelch-like
-
nadph:quinone
-
factor-2
-
lps-stimulated
-
2-like
-
erythroid-derived
-
oxygenases
-
delta-aminolevulinic
-
sulforaphane
-
hyperbilirubinemia
-
medicine
-
drug development
-
analysis
- 1.14.14.18
- monoxide
-
cytoprotective
- endothelial
- necrosis
- dismutase
- protoporphyrin
-
erythroid
-
2-related
- tnf
- bilirubin
- artery
- malondialdehyde
- lipopolysaccharide
- catalase
- hemin
-
neuroprotective
- ischemia
- gsh
- lps
- sod
-
anti-oxidant
- mapks
- sirna
- caspase-3
- quinone
- pulmonary
-
reperfusion
-
lps-induced
- hypoxia
- cyclooxygenase-2
- cox-2
- ferritin
- erk
-
nf-e2-related
-
anti-apoptotic
- cobalt
- myeloperoxidase
-
ischemia-reperfusion
-
nrf2-mediated
-
pro-oxidant
-
kelch-like
-
nadph:quinone
-
factor-2
-
lps-stimulated
-
2-like
-
erythroid-derived
- oxygenases
-
delta-aminolevulinic
- sulforaphane
- hyperbilirubinemia
- medicine
- drug development
- analysis
Reaction
+ 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = + + + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
Synonyms
biliverdin-producing heme oxygenase, ChuS, ChuZ, EC 1.14.99.3, haem oxygenase, heme oxygenase, heme oxygenase 1, heme oxygenase 2, heme oxygenase-1, heme oxygenase-2, HemO, Hmox1, Hmox1a, Hmox1b, Hmox2, Hmox2a, Hmox2b, HmuO, Hmx1, HO, HO-1, HO-2, Ho1, Ho2, Ho3, HO4, HSP32, HugZ, HY1, inducible heme oxygenase-1, More, MsHO1, ORP33 proteins, oxygenase, heme (decyclizing), pbsA1, PigA, proteins, specific or class, ORP33 (oxygen-regulated protein 33,000-mol.-wt.), Syn HO-1, Syn HO-2
ECTree
Advanced search results
Reaction
Reaction on EC 1.14.14.18 - heme oxygenase (biliverdin-producing)
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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