Redox properties of wild-type and heme-binding loop mutants of bacterial cytochromes c measured by direct electrochemistry

Inorganic Chemistry

Volumn 44, Issue 24, 2005, Pages 8999-9006

  Ye, Tao ^a   Kaur, Ravinder ^b   Wen, Xin ^b   Bren, Kara L ^b   Elliott, Sean J ^a  

^a Boston University   (United States)

^b UNIVERSITY OF ROCHESTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; BUFFER; CYTOCHROME C; HEME;

ARTICLE; BINDING SITE; ELECTROCHEMISTRY; ENZYMOLOGY; GENETICS; METABOLISM; METHODOLOGY; MUTATION; NITROSOMONAS EUROPAEA; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; OSMOLARITY; OXIDATION REDUCTION REACTION; PH; PROTEIN CONFORMATION; PSEUDOMONAS AERUGINOSA;

BACTERIAL PROTEINS; BINDING SITES; BUFFERS; CYTOCHROMES C; ELECTROCHEMISTRY; HEME; HYDROGEN-ION CONCENTRATION; MAGNETIC RESONANCE SPECTROSCOPY; MUTATION; NITROSOMONAS EUROPAEA; OSMOLAR CONCENTRATION; OXIDATION-REDUCTION; PROTEIN CONFORMATION; PSEUDOMONAS AERUGINOSA;

EID: 28844439342     PISSN: 00201669     EISSN: None     Source Type: Journal    
DOI: 10.1021/ic051003l     Document Type: Article

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