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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geprüft am 10.05.2024