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Volumn 288, Issue 43, 2013, Pages 31241-31249
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Aspartic acid 397 in subunit B of the Na+-pumping NADH:quinone oxidoreductase from Vibrio cholerae forms part of a sodium-binding site, is involved in cation selectivity, and affects cation-binding site cooperativity
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Author keywords
[No Author keywords available]
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Indexed keywords
ASPARTIC ACID RESIDUES;
ASPARTIC ACIDS;
CATION SELECTIVITY;
ELECTRON-TRANSFER STEP;
MUTANT ENZYMES;
OXIDOREDUCTASES;
PATHOGENIC BACTERIUM;
VIBRIO CHOLERAE;
BINDING SITES;
CELL MEMBRANES;
CYTOLOGY;
ENZYMES;
METAL IONS;
POSITIVE IONS;
PUMPS;
AMINO ACIDS;
ARGININE;
ASPARTIC ACID;
CATION;
CYSTEINE;
GLUTAMIC ACID;
LYSINE;
REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE;
REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE);
SERINE;
SODIUM ION;
UBIQUINONE;
ARTICLE;
BACTERIAL GROWTH;
BACTERIAL STRAIN;
BINDING SITE;
ELECTRON TRANSPORT;
ENZYME ACTIVITY;
ENZYME PURIFICATION;
MUTAGENESIS;
MUTANT;
NONHUMAN;
PRIORITY JOURNAL;
STEADY STATE;
VIBRIO CHOLERAE;
BACTERIA;
BACTERIAL METABOLISM;
BIOENERGETICS-ELECTRON TRANSFER COMPLEX;
REDOX;
SODIUM TRANSPORT;
AMINO ACID SUBSTITUTION;
ASPARTIC ACID;
BACTERIAL PROTEINS;
BINDING SITES;
ELECTRON TRANSPORT;
ION TRANSPORT;
MUTATION, MISSENSE;
QUINONE REDUCTASES;
SODIUM;
VIBRIO CHOLERAE;
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EID: 84886680239
PISSN: 00219258
EISSN: 1083351X
Source Type: Journal
DOI: 10.1074/jbc.M113.510776 Document Type: Article |
Times cited : (15)
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References (19)
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