Mutations in the putative H-channel in the cytochrome c oxidase from Rhodobacter sphaeroides show that this channel is not important for proton conduction but reveal modulation of the properties of heme a

Biochemistry

Volumn 39, Issue 11, 2000, Pages 2989-2996

  Lee, Hang Mo ^a   Das, Tapan Kanti ^b   Rousseau, Denis L ^b   Mills, Denise ^c   Ferguson Miller, Shelagh ^c   Gennis, Robert B ^a  

^a UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

^b ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

^c Michigan State University   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C OXIDASE; HEME; HYDROGEN;

ARTICLE; CHANNEL GATING; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME PURIFICATION; ENZYME STRUCTURE; HYDROGEN BOND; MOLECULAR INTERACTION; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEOLIPOSOME; PROTON TRANSPORT; RHODOBACTER SPHAEROIDES; SITE DIRECTED MUTAGENESIS; STRUCTURE ANALYSIS; X RAY ANALYSIS;

ALANINE; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; ARGININE; CATTLE; ELECTRON TRANSPORT COMPLEX IV; ENZYME ACTIVATION; GLUTAMINE; HEME; HISTIDINE; LYSINE; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTON PUMPS; RHODOBACTER SPHAEROIDES; SPECTRUM ANALYSIS, RAMAN; TYROSINE;

BACTERIA (MICROORGANISMS); BOVINAE; EUKARYOTA; MAMMALIA; PARACOCCUS DENITRIFICANS; PROKARYOTA; RHODOBACTER SPHAEROIDES; RHODOPSEUDOMONAS;

EID: 0034696637     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9924821     Document Type: Article

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