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36° step size of proton‐driven c ‐ring rotation in F o F 1 ‐ATP synthase
Author(s) -
Düser Monika G,
Zarrabi Nawid,
Cipriano Daniel J,
Ernst Stefan,
Glick Gary D,
Dunn Stanley D,
Börsch Michael
Publication year - 2009
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/emboj.2009.213
Subject(s) - atp synthase , biology , rotation (mathematics) , proton , ring (chemistry) , physics , enzyme , biochemistry , nuclear physics , artificial intelligence , chemistry , computer science , organic chemistry
Synthesis of adenosine triphosphate ATP, the ‘biological energy currency’, is accomplished by F o F 1 ‐ATP synthase. In the plasma membrane of Escherichia coli , proton‐driven rotation of a ring of 10 c subunits in the F o motor powers catalysis in the F 1 motor. Although F 1 uses 120° stepping during ATP synthesis, models of F o predict either an incremental rotation of c subunits in 36° steps or larger step sizes comprising several fast substeps. Using single‐molecule fluorescence resonance energy transfer, we provide the first experimental determination of a 36° sequential stepping mode of the c ‐ring during ATP synthesis.