ArticleBiochemistry2007
The crystal structure of cytochrome P460 of Nitrosomonas europaea reveals a novel cytochrome fold and heme-protein cross-link.
Article in Biochemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 53 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
- Review
- Outer coordination sphere influences on cofactor maturation and substrate oxidation by cytochrome P460.Chemical science · 2023Article
- Cytochrome P460 Cofactor Maturation Proceeds via Peroxide-Dependent Post-translational Modification.Journal of the American Chemical Society · 2023Article
- Mechanistic and structural characterization of an iridium-containing cytochrome reveals kinetically relevant cofactor dynamics.Nature catalysis · 2023Article
- Crystal structure of thermally stable homodimeric cytochrome c'-β from Thermus thermophilus.Acta crystallographica. Section F, Structural biology communications · 2022Article
- Heme P460: A (Cross) Link to Nitric Oxide.Accounts of chemical research · 2020Article
- Biological and Bioinspired Inorganic N-N Bond-Forming Reactions.Chemical reviews · 2020Review
- Controlling a burn: outer-sphere gating of hydroxylamine oxidation by a distal base in cytochrome P460.Chemical science · 2019Article
- One fold, two functions: cytochrome P460 and cytochromeChemical science · 2019Article
- The Eponymous Cofactors in Cytochrome P460s from Ammonia-Oxidizing Bacteria Are Iron Porphyrinoids Whose Macrocycles Are Dibasic.Biochemistry · 2018Article
- Influences of the heme-lysine crosslink in cytochrome P460 over redox catalysis and nitric oxide sensitivity.Chemical science · 2018Article
- Crystal structure and enzymatic properties of chalcone isomerase from the Antarctic vascular plant Deschampsia antarctica Desv.PloS one · 2018Article
- Characterization of plasma labile heme in hemolytic conditions.The FEBS journal · 2017Article
- 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
- Electron self-exchange and self-amplified posttranslational modification in the hemoglobins from Synechocystis sp. PCC 6803 and Synechococcus sp. PCC 7002.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2012Article
- 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 Desulfovibrio vulgaris dissimilatory sulfite reductase bound to DsrC provides novel insights into the mechanism of sulfate respiration.The Journal of biological chemistry · 2008Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
We have determined the 1.8 A X-ray crystal structure of a monoheme c-type cytochrome, cytochrome P460, from Nitrosomonas europea. The chromophore possesses unusual spectral properties analogous to those of the catalytic heme P460 of hydroxylamine oxidoreductase (HAO), the only known heme in biology to withdraw electrons from an iron-coordinated substrate. The analysis reveals a homodimeric structure and elucidates a new c-type cytochrome fold that is predominantly beta-sheet. In addition to the two cysteine thioether links to the porphyrin typical of c-type hemes, there is a third proteinaceous link involving a conserved lysine. The covalent bond is between the lysine side-chain nitrogen and the 13'-meso carbon of the heme, which, following cross-link formation, is sp3-hybridized, demonstrating the loss of conjugation at this position within the porphyrin. The structure has implications for the analogous tyrosine-heme meso carbon cross-link observed in HAO.
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