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Volumn 273, Issue 48, 1999, Pages 31916-31923
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The quinone-binding site in succinate-ubiquinone reductase from Escherichia coli: Quinone-binding domain and amino acid residues involved in quinone binding
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Author keywords
[No Author keywords available]
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Indexed keywords
1,4 BENZOQUINONE;
AMINO ACID;
CARBONYL DERIVATIVE;
HYDROGEN;
HYDROXYL GROUP;
PROTEINASE;
SUCCINATE DEHYDROGENASE (UBIQUINONE);
AMINO ACID SEQUENCE;
AMINO ACID SUBSTITUTION;
AMINO TERMINAL SEQUENCE;
ARTICLE;
BINDING AFFINITY;
BINDING SITE;
ENZYME ACTIVITY;
ESCHERICHIA COLI;
GENE;
HIGH PERFORMANCE LIQUID CHROMATOGRAPHY;
NONHUMAN;
POLYACRYLAMIDE GEL ELECTROPHORESIS;
PRIORITY JOURNAL;
AFFINITY LABELS;
AMINO ACID SEQUENCE;
AMINO ACID SUBSTITUTION;
AZIDES;
BASE SEQUENCE;
BENZOQUINONES;
BINDING SITES;
CHROMOSOME MAPPING;
CHROMOSOMES, BACTERIAL;
ELECTRON TRANSPORT COMPLEX II;
ESCHERICHIA COLI;
KINETICS;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
MULTIENZYME COMPLEXES;
MUTAGENESIS, SITE-DIRECTED;
OLIGODEOXYRIBONUCLEOTIDES;
OPERON;
OXIDOREDUCTASES;
PEPTIDE FRAGMENTS;
POINT MUTATION;
PROTEIN STRUCTURE, SECONDARY;
RECOMBINANT PROTEINS;
SUCCINATE DEHYDROGENASE;
UBIQUINONE;
BACTERIA (MICROORGANISMS);
ESCHERICHIA COLI;
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EID: 0033610898
PISSN: 00219258
EISSN: None
Source Type: Journal
DOI: 10.1074/jbc.273.48.31916 Document Type: Article |
Times cited : (49)
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References (25)
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