1.7.2.6: hydroxylamine dehydrogenase
This is an abbreviated version!
For detailed information about hydroxylamine dehydrogenase, go to the full flat file.
Word Map on EC 1.7.2.6
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1.7.2.6
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ammonia
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monooxygenase
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nitrification
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metagenomic
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nitrify
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nitrospira
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europaea
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no2
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nitrosomonas
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comammox
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phenylhydrazine
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ammonium-oxidizing
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genome-centric
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analysis
- 1.7.2.6
- ammonia
- monooxygenase
-
nitrification
-
metagenomic
-
nitrify
- nitrospira
- europaea
- no2
- nitrosomonas
-
comammox
- phenylhydrazine
-
ammonium-oxidizing
-
genome-centric
- analysis
Reaction
+ + 4 ferricytochrome c = + 4 ferrocytochrome c + 5 H+
Synonyms
EC 1.7.3.4, HAO, haoA, HCR, HOA, hydroxylamine cytochrome c554 oxidoreductase, hydroxylamine oxidase, hydroxylamine oxidoreductase, hydroxylamine-cytochrome c reductase, hydroxylamine:oxygen oxidoreductase, mHAO, NeHAO, NirK, NoHAO
ECTree
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Cofactor
Cofactor on EC 1.7.2.6 - hydroxylamine dehydrogenase
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cytochrome c
purified enzyme shows typical cytochrome-like absorption spectra, but with a peculiar peak at 468 nm in the reduced state that is due to a P460 moiety corresponding to a modified heme c molecule
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heme
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each alpha,beta subunit of the (alpha,beta)3 subunit structure contains 7-8 c-type hemes and one prosthetic group P-460, P-460 is a MW 17000 protein fragment
heme
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resolution of the hemes by redox potentiometry and electron spin resonance spectroscopy
heme
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enzyme consists of one alpha-beta-3 subunit and contains seven-eight c-type hemes and P460
heme
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8 hemes per subunit: a triheme cluster, four hemes that are electronically coupled in two distinguishable pairs and one of these pairs is at the active site, and one heme that is not part of a cluster
heme
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multi-heme enzyme containing at least 5 thermodynamically distinct c-type hemes and the heme-like moiety P460
heme
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resolution of multiple heme centers by electron paramagnetic resonance spectroscopy
heme
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contains hemes c-553, c-559 and P-460 in the ratio 5:2:1, P-460 is the site of electron entry
heme
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each subunit of the enzyme contains 7 c-hemes and 1 heme P460. The latter, a c-heme crosslinked from a methylene carbon to the ring of a protein tyrosine, forms part of the active site
heme
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contains seven C-type hemes and one P460-type heme per alphabeta subunit
heme
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each subunit contains eight c-type hemes (inclusive one P460 heme)
heme
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each subunit contains seven c-type hemes and an eighth heme known as P460
heme
the enzyme contains 24 hemes, localized in four clusters within each monomer
heme
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the enzyme contains eight hemes per subunit, seven C-type cytochromes and one heme P460
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each monomer contains 7 c-type hemes and a novel heme known as P460, the role of the c-hemes appears to be the transfer of electrons from the P460 active site to 1 or more electron acceptors, cytochrome c554 is the most likely candidate as the electron acceptor
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additional information
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hydroxylamine oxidation takes place on three novel hemes known as P460
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