ArticleJournal of bacteriology1994
Oxidation of hydroxylamine by cytochrome P-460 of the obligate methylotroph Methylococcus capsulatus Bath.
Article in Journal of bacteriology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 62 citations in OpenAlex.
- Cytochromes P460 and c'-β: exploiting a novel fold for multiple functions.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025Review
- Plant microbiomes harbor potential to promote nutrient turnover in impoverished substrates of a Brazilian biodiversity hotspot.The ISME journal · 2023Article
- Heme P460: A (Cross) Link to Nitric Oxide.Accounts of chemical research · 2020Article
- Simultaneous nitrification-denitrification by phosphate accumulating microorganisms.World journal of microbiology & biotechnology · 2020Review
- Biological and Bioinspired Inorganic N-N Bond-Forming Reactions.Chemical reviews · 2020Review
- One fold, two functions: cytochrome P460 and cytochromeChemical science · 2019Article
- Influences of the heme-lysine crosslink in cytochrome P460 over redox catalysis and nitric oxide sensitivity.Chemical science · 2018Article
- Rare Earth Elements Alter Redox Balance inFrontiers in microbiology · 2018Article
- Nitric oxide is an obligate bacterial nitrification intermediate produced by hydroxylamine oxidoreductase.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Is there a pathway for N2O production from hydroxylamine oxidoreductase in ammonia-oxidizing bacteria?Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Nitrosomonas europaea cytochrome P460 is a direct link between nitrification and nitrous oxide emission.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Transcriptomic profiling of Methylococcus capsulatus (Bath) during growth with two different methane monooxygenases.MicrobiologyOpen · 2016Article
- Genome analysis coupled with physiological studies reveals a diverse nitrogen metabolism in Methylocystis sp. strain SC2.PloS one · 2013Article
- Crystallization and preliminary X-ray crystallographic analysis of a new crystal form of hydroxylamine oxidoreductase from Nitrosomonas europaea.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009Article
- The crystal structure of cytochrome P460 of Nitrosomonas europaea reveals a novel cytochrome fold and heme-protein cross-link.Biochemistry · 2007Article
- Complete genome sequence of the marine, chemolithoautotrophic, ammonia-oxidizing bacterium Nitrosococcus oceani ATCC 19707.Applied and environmental microbiology · 2006Article
- Expression, purification, crystallization and preliminary X-ray diffraction of a novel Nitrosomonas europaea cytochrome, cytochrome P460.Acta crystallographica. Section F, Structural biology and crystallization communications · 2006Article
- High-molecular-mass multi-c-heme cytochromes from Methylococcus capsulatus bath.Journal of bacteriology · 1999Article
- Cytochrome P460 genes from the methanotroph Methylococcus capsulatus bath.Journal of bacteriology · 1998Article
- Hydroxylamine oxidation in heterotrophic nitrate-reducing soil bacteria and purification of a hydroxylamine-cytochrome c oxidoreductase from a Pseudomonas species.Archives of microbiology · 1996Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
An enzyme capable of the oxidation of hydroxylamine to nitrite was isolated from the obligate methylotroph Methylococcus capsulatus Bath. The absorption spectra in cell extracts, electron paramagnetic resonance spectra, molecular weight, covalent attachment of heme group to polypeptide, and enzymatic activities suggest that the enzyme is similar to cytochrome P-460, a novel iron-containing protein previously observed only in Nitrosomonas europaea. The native and subunit molecular masses of the M. capsulatus Bath protein were 38,900 and 16,390 Da, respectively; the isoelectric point was 6.98. The enzyme has approximately one iron and one copper atom per subunit. The electron paramagnetic resonance spectrum of the protein showed evidence for a high-spin ferric heme. In contrast to the enzyme from N. europaea, a 13-nm blue shift in the soret band of the ferrocytochrome (463 nm in cell extracts to 450 nm in the final sample) occurred during purification. The amino acid composition and N-terminal amino acid sequence of the enzyme from M. capsulatus Bath was similar but not identical to those of cytochrome P-460 of N. europaea. In cell extracts, the identity of the biological electron acceptor is as yet unestablished. Cytochrome c-555 is able to accept electrons from cytochrome P-460, although the purified enzyme required phenazine methosulfate for maximum hydroxylamine oxidation activity (specific activity, 366 mol of O2 per s per mol of enzyme). Hydroxylamine oxidation rates were stimulated approximately 2-fold by 1 mM cyanide and 1.5-fold by 0.1 mM 8-hydroxyquinoline.
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