Role of the conserved arginine 274 and histidine 224 and 228 residues in the NuoCD subunit of complex I from Escherichia coli

Biochemistry

Volumn 46, Issue 2, 2007, Pages 526-533

  Belevich, Galina ^a   Euro, Liliya ^a   Wikström, Mårten ^a   Verkhovskaya, Marina ^a  

^a UNIVERSITY OF HELSINKI   (Finland)

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; COMPLEXATION; ENZYME INHIBITION; ENZYMES; ESCHERICHIA COLI; PURIFICATION;

ALANINE; ARGININE 274; HISTIDINE 224; UBIQUINONE REDUCTASE;

AMINO ACIDS;

ALANINE; ARGININE; BULLATACIN; DITHIONITE; HISTIDINE; LIPOSOME; MUTANT PROTEIN; QUINONE DERIVATIVE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); SUPEROXIDE; UBIQUINONE;

AMINO ACID SUBSTITUTION; ARTICLE; BACTERIAL STRAIN; BINDING SITE; CONTROLLED STUDY; ELECTRIC POTENTIAL; ELECTRON SPIN RESONANCE; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME SUBUNIT; ESCHERICHIA COLI; MUTATION; NONHUMAN; PLASMID; PRIORITY JOURNAL; PROTEIN EXPRESSION; REDUCTION;

AMINO ACID SUBSTITUTION; ARGININE; BASE SEQUENCE; CONSERVED SEQUENCE; DNA, BACTERIAL; ELECTRON SPIN RESONANCE SPECTROSCOPY; ELECTRON TRANSPORT COMPLEX I; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HISTIDINE; KINETICS; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; PROTEIN SUBUNITS;

ESCHERICHIA COLI;

EID: 33846240878     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi062062t     Document Type: Article

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