Replacement of lysine 45 by uncharged residues modulates the redox-Bohr effect in tetraheme cytochrome c3 of Desulfovibrio vulgaris (Hildenborough)

Biochemistry

Volumn 37, Issue 35, 1998, Pages 12160-12165

  Saraiva, Lígia M ^a   Salgueiro, Carlos A ^a   Da Costa, Patrícia N ^a   Messias, Ana C ^a   LeGall, Jean ^b   Van Dongen, Walter M A M ^c   Xavier, António V ^a  

^a INSTITUTO DE TECNOLOGIA QUÍMICA E BIOLÓGICA   (Portugal)

^b University of Georgia ^*  (United States)

^c WAGENINGEN UNIVERSITY   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C3; LYSINE;

ANALYTIC METHOD; ARTICLE; BOHR EFFECT; CONFORMATIONAL TRANSITION; DESULFOVIBRIO VULGARIS; ELECTRON TRANSPORT; ENZYME MODIFICATION; HYDROGEN BOND; MOLECULAR INTERACTION; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTON NUCLEAR MAGNETIC RESONANCE; SITE DIRECTED MUTAGENESIS;

AMINO ACID SUBSTITUTION; CYTOCHROME C GROUP; DESULFOVIBRIO VULGARIS; ELECTRON TRANSPORT; HEME; LYSINE; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; OXIDATION-REDUCTION; PROTEIN CONFORMATION; SPECTROPHOTOMETRY; THERMODYNAMICS;

DESULFOVIBRIO VULGARIS;

EID: 0032169524     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi981001v     Document Type: Article

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