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ATP Synthesis by Rotary Catalysis (Nobel lecture)
Author(s) -
Walker John E.
Publication year - 1998
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/(sici)1521-3773(19980918)37:17<2308::aid-anie2308>3.0.co;2-w
Subject(s) - protein subunit , atp synthase gamma subunit , conformational change , atp synthase , chemistry , biophysics , nucleotide , enzyme , catalysis , stereochemistry , crystallography , alternation (linguistics) , biochemistry , biology , atpase , atp hydrolysis , gene , linguistics , philosophy
The cyclic modulation of nucleotide‐binding properties of the three catalytic β subunits by a series of conformational changes was an attractive explanation for the postulated binding change mechanism of ATP synthase. In the crystal structure of the catalytic F 1 domain of this enzyme there is indeed a complex made up of three α subunits and three β subunits arranged in alternation around a central α ‐helical segment of the γ subunit. This complex is asymmetric owing to the different conformations of the β subunits. The change in conformation is brought about by rotation of the rigid yet curved segment, which has meanwhile been proven experimentally.