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Volumn 32, Issue 5, 2000, Pages 531-538
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Inhibitory Mg-ADP-fluoroaluminate complexes bound to catalytic sites of F1-ATPases: Are they ground-state or transition-state analogs?
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Author keywords
F1 ATPase; Ground state analog; Rotational catalysis; Transition state analog
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Indexed keywords
ADENOSINE DIPHOSPHATE;
ADENOSINE TRIPHOSPHATASE;
ADENOSINE TRIPHOSPHATE;
FLUOROALUMINATE;
MAGNESIUM DERIVATIVE;
NUCLEOTIDE;
ENZYME ACTIVE SITE;
ENZYME KINETICS;
ENZYME MECHANISM;
HYDROLYSIS;
ROTATION;
SHORT SURVEY;
SYNTHESIS;
ADENOSINE DIPHOSPHATE;
ALUMINUM;
CATALYTIC DOMAIN;
FLUORINE;
KINETICS;
MODELS, BIOLOGICAL;
MODELS, MOLECULAR;
MUTAGENESIS, SITE-DIRECTED;
PROTEIN SUBUNITS;
PROTON-TRANSLOCATING ATPASES;
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EID: 0034466410
PISSN: 0145479X
EISSN: None
Source Type: Journal
DOI: 10.1023/A:1005677310791 Document Type: Short Survey |
Times cited : (9)
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References (46)
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