Covalent modification of the catalytic sites of the H+-ATPase from chloroplasts, CF0F1, with 2-azido-[α-32P]ADP: Modification of the catalytic site 2 (loose) and the catalytic site 3 (open) impairs multi-site, but not uni-site catalysis of both ATP synthesis and ATP hydrolysis

Biochimica et Biophysica Acta - Bioenergetics

Volumn 1456, Issue 2-3, 2000, Pages 77-98

  Possmayer, Franziska E ^a,b   Hartog, Aloysius F ^b   Berden, Jan A ^b   Gräber, Peter ^a  

^a UNIVERSITY OF FREIBURG   (Germany)

^b UNIVERSITY OF AMSTERDAM   (Netherlands)

Author keywords

2 Azido nucleotide; CF0F1; H+ATPase; Nucleotide binding; Uni site catalysis

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; LIPOSOME; NUCLEOTIDE;

ARTICLE; BINDING SITE; CATALYSIS; CHLOROPLAST; COVALENT BOND; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; SYNTHESIS; ULTRAVIOLET RADIATION;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; AZIDES; CATALYTIC DOMAIN; CHLOROPLASTS; HYDROLYSIS; KINETICS; LIPOSOMES; PHOSPHORUS RADIOISOTOPES; PHOTOAFFINITY LABELS; PROTEIN BINDING; PROTON-TRANSLOCATING ATPASES;

EID: 0033980598     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2728(99)00106-1     Document Type: Article

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