The coupling of the relative movement of the a and c subunits of the F0 to the conformational changes in the F1-ATPase.
F0F1-ATPase structural information gained from X-ray crystallography and electron microscopy has activated interest in a rotational mechanism for the F0F1-ATPase. Because of the subunit stoichiometry and the involvement of both a- and c-subunits in the mechanism of proton movement, it is argued that relative movement must occur between the subunits. Various options for the arrangement and structure of the subunits involved are discussed and a mechanism proposed.
Howitt
S M
SM
Division of Biochemistry and Molecular Biology, John Curtin School of Medical Research, Australian National University, Canberra.
Rodgers
A J
AJ
Hatch
L P
LP
Gibson
F
F
Cox
G B
GB
D001692:Biological Transport; D004926:Escherichia coli / Q000201:enzymology; D011487:Protein Conformation; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000378:metabolism*; D011522:Protons; D013329:Structure-Activity Relationship
D011522:Protons; D006180:Proton-Translocating ATPases