Specific tryptophan substitution in catalytic sites of Escherichia coli F1-ATPase allows differentiation between bound substrate ATP and product ADP in steady-state catalysis

Journal of Biological Chemistry

Volumn 271, Issue 31, 1996, Pages 18711-18718

  Weber, Joachim ^a   Bowman, Cheryl ^a   Senior, Alan E ^a  

^a UNIVERSITY OF ROCHESTER MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ADENOSINE TRIPHOSPHATE MAGNESIUM; NUCLEOTIDE; NUCLEOTIDE BINDING PROTEIN; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; TRYPTOPHAN;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; ENZYME ACTIVE SITE; ESCHERICHIA COLI; FLUORESCENCE; NONHUMAN; PRIORITY JOURNAL; STEADY STATE;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ADENYLYL IMIDODIPHOSPHATE; BASE SEQUENCE; BINDING SITES; CATALYSIS; ESCHERICHIA COLI; FLUORESCENT DYES; HYDROLYSIS; KINETICS; MAGNESIUM; MODELS, BIOLOGICAL; MOLECULAR SEQUENCE DATA; MUTAGENESIS, INSERTIONAL; OLIGODEOXYRIBONUCLEOTIDES; PROTON-TRANSLOCATING ATPASES; SPECTROMETRY, FLUORESCENCE; SUBSTRATE SPECIFICITY; TRYPTOPHAN;

EID: 0029744684     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.271.31.18711     Document Type: Article

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