The α3(βY341W)3γ subcomplex of the F1-ATpase from the thermophilic Bacillus PS3 fails to dissociate ADP when MgATP is hydrolyzed at a single catalytic site and attains maximal velocity when three catalytic sites are saturated with MgATP

Biochemistry

Volumn 37, Issue 47, 1998, Pages 16757-16764

  Dou, Chao ^a   Fortes, P A George ^a   Allison, William S ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE MAGNESIUM; MAGNESIUM; OXIDE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; TRYPTOPHAN;

ARTICLE; BACILLUS; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVITY; FLUORESCENCE; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS; STOICHIOMETRY; VELOCITY;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ANIMALS; AZIDES; BACILLUS; BINDING SITES; CATALYSIS; CATTLE; CROSS-LINKING REAGENTS; DETERGENTS; DIMETHYLAMINES; FLUORESCENCE POLARIZATION; HYDROLYSIS; KINETICS; MUTAGENESIS, SITE-DIRECTED; PROTON-TRANSLOCATING ATPASES; SPECTROMETRY, FLUORESCENCE; TRYPTOPHAN; TYROSINE;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0032564377     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi981717q     Document Type: Article

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