Enzymes
| UniProtKB help_outline | 164 proteins |
| Enzyme class help_outline |
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Reaction participants Show >> << Hide
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Namehelp_outline
Fe(III)-[cytochrome c]
Identifier
RHEA-COMP:14399
Reactive part
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- Name help_outline Fe3+ Identifier CHEBI:29034 (CAS: 20074-52-6) help_outline Charge 3 Formula Fe InChIKeyhelp_outline VTLYFUHAOXGGBS-UHFFFAOYSA-N SMILEShelp_outline [Fe+3] 2D coordinates Mol file for the small molecule Search links Involved in 234 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,048 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline hydroxylamine Identifier CHEBI:15429 (CAS: 7803-49-8) help_outline Charge 0 Formula H3NO InChIKeyhelp_outline AVXURJPOCDRRFD-UHFFFAOYSA-N SMILEShelp_outline NO 2D coordinates Mol file for the small molecule Search links Involved in 13 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
Fe(II)-[cytochrome c]
Identifier
RHEA-COMP:10350
Reactive part
help_outline
- Name help_outline Fe2+ Identifier CHEBI:29033 (CAS: 15438-31-0) help_outline Charge 2 Formula Fe InChIKeyhelp_outline CWYNVVGOOAEACU-UHFFFAOYSA-N SMILEShelp_outline [Fe++] 2D coordinates Mol file for the small molecule Search links Involved in 250 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,176 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline nitrite Identifier CHEBI:16301 (CAS: 14797-65-0) help_outline Charge -1 Formula NO2 InChIKeyhelp_outline IOVCWXUNBOPUCH-UHFFFAOYSA-M SMILEShelp_outline [O-]N=O 2D coordinates Mol file for the small molecule Search links Involved in 65 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:45032 | RHEA:45033 | RHEA:45034 | RHEA:45035 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Studies of the hydroxylamine metabolism of Nitrosomonas europaea. I. Purification of hydroxylamine oxidase.
Rees M.K.
Biochemistry 7:353-366(1968) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Hydroxylamine oxidoreductase of Nitrosomonas. Production of nitric oxide from hydroxylamine.
Hooper A.B., Terry K.R.
Biochim. Biophys. Acta 571:12-20(1979) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Transcription of nitrification genes by the methane-oxidizing bacterium, Methylococcus capsulatus strain Bath.
Poret-Peterson A.T., Graham J.E., Gulledge J., Klotz M.G.
Methylococcus capsulatus strain Bath, a methane-oxidizing bacterium, and ammonia-oxidizing bacteria (AOB) carry out the first step of nitrification, the oxidation of ammonia to nitrite, through the intermediate hydroxylamine. AOB use hydroxylamine oxidoreductase (HAO) to produce nitrite. M. capsul ... >> More
Methylococcus capsulatus strain Bath, a methane-oxidizing bacterium, and ammonia-oxidizing bacteria (AOB) carry out the first step of nitrification, the oxidation of ammonia to nitrite, through the intermediate hydroxylamine. AOB use hydroxylamine oxidoreductase (HAO) to produce nitrite. M. capsulatus Bath was thought to oxidize hydroxylamine with cytochrome P460 (cytL), until the recent discovery of an hao gene in its genome. We used quantitative PCR analyses of cDNA from M. capsulatus Bath incubated with CH(4) or CH(4) plus 5 mM (NH(4))(2)SO(4) to determine whether cytL and hao transcript levels change in response to ammonia. While mRNA levels for cytL were not affected by ammonia, hao mRNA levels increased by 14.5- and 31-fold in duplicate samples when a promoter proximal region of the transcript was analyzed, and by sixfold when a region at the distal end of the transcript was analyzed. A conserved open reading frame, orf2, located 3' of hao in all known AOB genomes and in M. capsulatus Bath, was cotranscribed with hao and showed increased mRNA levels in the presence of ammonia. These data led to designating this gene pair as haoAB, with the role of haoB still undefined. We also determined mRNA levels for additional genes that encode proteins involved in N-oxide detoxification: cytochrome c'-beta (CytS) and nitric oxide (NO) reductase (NorCB). Whereas cytS mRNA levels increased in duplicate samples by 28.5- and 40-fold in response to ammonia, the cotranscribed norC-norB mRNA did not increase. Our results strongly suggest that M. capsulatus Bath possesses a functional, ammonia-responsive HAO involved in nitrification. << Less
ISME J 2:1213-1220(2008) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.