Evidence for a crosslink betweenc-heme and a lysine residue in cytochrome P460 ofNitrosomonas europaea
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/S0014-5793(97)00635-2/fullpdf
Reference10 articles.
1. Characterization of Hydroxylamine-Cytochrome c Reductase from the Chemoautotrophs Nitrosomonas europaea and Nitrosocystis oceanus
2. Preliminary characterization of a variant co-binding heme protein from Nitrosomonas
3. Hydroxylamine oxidoreductase from Nitrosomonas europaea is a multimer of an octa-heme subunit
4. Characterization of the gene encoding hydroxylamine oxidoreductase in Nitrosomonas europaea
5. Evidence for the structure of the active site heme P460 in hydroxylamine oxidoreductase of Nitrosomonas
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1. Role of Nitric Oxide in Hydroxylamine Oxidation by Ammonia-Oxidizing Bacteria;Applied and Environmental Microbiology;2023-08-30
2. The Heme–Lys Cross-Link in Cytochrome P460 Promotes Catalysis by Enforcing Secondary Coordination Sphere Architecture;Biochemistry;2020-06-11
3. Cytochrome c′β-Met Is a Variant in the P460 Superfamily Lacking the Heme–Lysyl Cross-Link: A Peroxidase Mimic Generating a Ferryl Intermediate;Biochemistry;2019-12-30
4. The Discovery of Twenty-Eight New Encapsulin Sequences, Including Three in Anammox Bacteria;Scientific Reports;2019-12
5. The Eponymous Cofactors in Cytochrome P460s from Ammonia-Oxidizing Bacteria Are Iron Porphyrinoids Whose Macrocycles Are Dibasic;Biochemistry;2017-12-06
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