The role of arginine-127 at the proximal NO-binding site in determining the electronic structure and function of 5-coordinate NO-heme in cytochrome c' of Rhodobacter sphaeroides.

Journal article

Cytochrome c' is a heme protein from a denitrifying variant of Rhodobacter sphaeroides which may serve to store and transport metabolic NO while protecting against NO toxicity. Its heme site bears resemblance through its 5-coordinate NO-binding capability to the regulatory site in soluble guanylate cyclase. A conserved arginine (Arg-127) abuts the 5-coordinate NO-heme binding site, and the alanine mutant R127A provided insight into the role of the Arg-127 in establishing the electronic struct...

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Authors: Lee, B; Usov, O; Grigoryants, V; Myers, W; Shapleigh, J

• Publication status: Published
• Journal: Biochemistry
• Volume: 48
• Issue: 38
• Pages: 8985-8993
• Publication date: 2009-09-01
• DOI: 10.1021/bi900833f
• EISSN: 1520-4995
• ISSN: 0006-2960
• Language: English
• Keywords: Mutagenesis, Site-Directed; Nitric Oxide; Bacterial Proteins; Binding Sites; Oxidation-Reduction; Amino Acid Substitution; Kinetics; Electron Spin Resonance Spectroscopy; Heme; Arginine; Recombinant Proteins; Cytochromes c'; Rhodobacter sphaeroides; Static Electricity; Spectrophotometry; Models, Molecular