ArticleBiochemistry2018
The Eponymous Cofactors in Cytochrome P460s from Ammonia-Oxidizing Bacteria Are Iron Porphyrinoids Whose Macrocycles Are Dibasic.
Article in Biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed.
- 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
- Nitrification Mechanisms for the P460 Enzymes.The journal of physical chemistry. B · 2025Article
- Characterisation of bacteria representing a novel Nitrosomonas clade: Physiology, genomics and distribution of missing ammonia oxidizer.Environmental microbiology reports · 2023Article
- Mechanistic and structural characterization of an iridium-containing cytochrome reveals kinetically relevant cofactor dynamics.Nature catalysis · 2023Article
- 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
- Formation and Reactivity of New Isoporphyrins: Implications for Understanding the Tyr-His Cross-Link Cofactor Biogenesis in CytochromeJournal of the American Chemical Society · 2019Article
- 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
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
The enzymes hydroxylamine oxidoreductase and cytochrome (cyt) P460 contain related unconventional "heme P460" cofactors. These cofactors are unusual in their inclusion of nonstandard cross-links between amino acid side chains and the heme macrocycle. Mutagenesis studies performed on the Nitrosomonas europaea cyt P460 that remove its lysine-heme cross-link show that the cross-link is key to defining the spectroscopic properties and kinetic competence of the enzyme. However, exactly how this cross-link confers these features remains unclear. Here we report the 1.45 Å crystal structure of cyt P460 from Nitrosomonas sp. AL212 and conclude that the cross-link does not lead to a change in hybridization of the heme carbon participating in the cross-link but rather enforces structural distortions to the macrocycle away from planarity. Time-dependent density functional theory coupled to experimental structural and spectroscopic analysis suggest that this geometric distortion is sufficient to define the spectroscopic properties of the heme P460 cofactor and provide clues toward establishing a relationship between heme P460 electronic structure and function.
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Registered trials
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