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Volumn 39, Issue 31, 2000, Pages 9583-9590
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New probes of the F1-ATPase catalytic transition state reveal that two of the three catalytic sites can assume a transition state conformation simultaneously
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Author keywords
[No Author keywords available]
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Indexed keywords
ADENOSINE DIPHOSPHATE;
FLUORIDE;
MAGNESIUM;
PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;
SCANDIUM;
ARGININE;
ENZYME INHIBITOR;
GLUTAMINE;
INOSINE DIPHOSPHATE;
LYSINE;
PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE;
TRYPTOPHAN;
TYROSINE;
ARTICLE;
BINDING AFFINITY;
CATALYSIS;
CONFORMATION;
ENZYME ACTIVE SITE;
ENZYME ACTIVITY;
ENZYME INHIBITION;
HYDROLYSIS;
PRIORITY JOURNAL;
BINDING SITE;
CHEMISTRY;
DRUG ANTAGONISM;
DRUG EFFECT;
DRUG POTENTIATION;
ENZYME ACTIVATION;
ENZYMOLOGY;
ESCHERICHIA COLI;
GENETICS;
PROTEIN CONFORMATION;
SITE DIRECTED MUTAGENESIS;
SPECTROFLUOROMETRY;
TITRIMETRY;
ADENOSINE DIPHOSPHATE;
ARGININE;
BINDING SITES;
CATALYSIS;
DRUG SYNERGISM;
ENZYME ACTIVATION;
ENZYME INHIBITORS;
ESCHERICHIA COLI;
GLUTAMINE;
INOSINE DIPHOSPHATE;
LYSINE;
MUTAGENESIS, SITE-DIRECTED;
PROTEIN CONFORMATION;
PROTON-TRANSLOCATING ATPASES;
SCANDIUM;
SPECTROMETRY, FLUORESCENCE;
TITRIMETRY;
TRYPTOPHAN;
TYROSINE;
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EID: 0034622430
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi000941o Document Type: Article |
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Times cited : (28)
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References (51)
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