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

Biochemistry

Volumn 48, Issue 38, 2009, Pages 8985-8993

  Lee, Byunghoon ^a   Usov, Oleg M ^a   Grigoryants, Vladimir M ^a   Myers, William K ^a   Shapleigh, James P ^b   Scholes, Charles P ^a  

^a STATE UNIVERSITY OF NEW YORK   (United States)

^b Department of Obstetrics Gynecology   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING AFFINITIES; BINDING CAPABILITY; BOND ANGLE; CYTOCHROME C; ELECTRON NUCLEAR DOUBLE RESONANCE; G-VALUES; GUANYLATE CYCLASE; HEME BINDING; HEME PROTEINS; HYDROGEN BONDINGS; HYPERFINE COUPLING; HYPERFINES; N-O COMPLEXES; POSITIVELY CHARGED; REDOX POTENTIALS; RHODOBACTER SPHAEROIDES; WILD TYPES; WILD-TYPE PROTEINS;

AMINO ACIDS; BINDING ENERGY; DEUTERIUM; ELECTRONIC PROPERTIES; ELECTRONIC STRUCTURE; HEMOGLOBIN; HYDROGEN; HYDROGEN BONDS; NUCLEAR MAGNETIC RESONANCE; PORPHYRINS; SECONDARY BATTERIES;

BINDING SITES;

ALANINE; ARGININE; CYTOCHROME C; GUANYLATE CYCLASE; HEME; NITROUS OXIDE; PHENYLALANINE; BACTERIAL PROTEIN; CYTOCHROME C'; NITRIC OXIDE; RECOMBINANT PROTEIN;

ARTICLE; BINDING AFFINITY; BINDING SITE; ELECTRON NUCLEAR DOUBLE RESONANCE; HYDROGEN BOND; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN STRUCTURE; RHODOBACTER SPHAEROIDES; AMINO ACID SUBSTITUTION; CHEMICAL STRUCTURE; CHEMISTRY; ELECTRON SPIN RESONANCE; GENETICS; KINETICS; METABOLISM; SITE DIRECTED MUTAGENESIS; SPECTROPHOTOMETRY; STATIC ELECTRICITY;

RHODOBACTER SPHAEROIDES;

AMINO ACID SUBSTITUTION; ARGININE; BACTERIAL PROTEINS; BINDING SITES; CYTOCHROMES C'; ELECTRON SPIN RESONANCE SPECTROSCOPY; HEME; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; NITRIC OXIDE; OXIDATION-REDUCTION; RECOMBINANT PROTEINS; RHODOBACTER SPHAEROIDES; SPECTROPHOTOMETRY; STATIC ELECTRICITY;

EID: 70349785611     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi900833f     Document Type: Article

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