ATP Synthase

Autor(en): Junge, Wolfgang 
Nelson, Nathan
Herausgeber: Kornberg, RD
Stichwörter: 3 CATALYTIC SITES; ATP synthesis; Biochemistry & Molecular Biology; C SUBUNIT OLIGOMER; chloroplasts; cyanobacteria; ELASTIC POWER TRANSMISSION; ENERGY TRANSDUCTION; ESCHERICHIA-COLI; FOF1 ATPase; GAMMA-SUBUNIT; OXIDATIVE-PHOSPHORYLATION; photosynthesis; proton transfer; ROTARY F-ATPASE; THYLAKOID MEMBRANES; TORQUE GENERATION
Erscheinungsdatum: 2015
Herausgeber: ANNUAL REVIEWS
Journal: ANNUAL REVIEW OF BIOCHEMISTRY, VOL 84
Annual Review of Biochemistry
Volumen: 84
Startseite: 631
Seitenende: 657
Zusammenfassung: 
Oxygenic photosynthesis is the principal converter of sunlight into chemical energy. Cyanobacteria and plants provide aerobic life with oxygen, food, fuel, fibers, and platform chemicals. Four multisubunit membrane proteins are involved: photosystem I (PSI), photosystem II (PSII), cytochrome b(6)f (cyt b(6)f), and ATP synthase (FOF1). ATP synthase is likewise a key enzyme of cell respiration. Over three billion years, the basic machinery of oxygenic photosynthesis and respiration has been perfected to minimize wasteful reactions. The proton-driven ATP synthase is embedded in a proton tight-coupling membrane. It is composed of two rotary motors/generators, F-O and F-1, which do not slip against each other. The proton-driven FO and the ATP-synthesizing F-1 are coupled via elastic torque transmission. Elastic transmission decouples the two motors in kinetic detail but keeps them perfectly coupled in thermodynamic equilibrium and (time-averaged) under steady turnover. Elastic transmission enables operation with different gear ratios in different organisms.
ISBN: 9780824308841
ISSN: 00664154
DOI: 10.1146/annurev-biochem-060614-034124

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