New results about structure, function and regulation of the chloroplast ATP synthase (CF0CF1)
Georg Groth, Heinrich Strotmann
Abstract
Georg Groth, Heinrich Strotmann
Abstract
The chloroplast ATP synthase utilises the energy of a transmembrane electrochemical proton gradient to drive the synthesis of ATP from ADP and phosphate. This multi‐subunit thylakoid membrane‐bound enzyme consists of a proton channel, CF0, and an extrinsic catalytic sector, CF1. Stimulated by the elucidation of a three‐dimensional partial structure of the mitochondrial enzyme, substantial progress has been made to understand the catalytic mechanism and interesting hypotheses have been proposed about the molecular mechanism of energy coupling. The review discusses the present state of knowledge concerning the structure, molecular genetics, catalytic mechanism, energy coupling and regulation of this important enzyme involved in photophosphorylation.
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The chloroplast ATP synthase utilises the energy of a transmembrane electrochemical proton gradient to drive the synthesis of ATP from ADP and phosphate. This multi‐subunit thylakoid membrane‐bound enzyme consists of a proton channel, CF0, and an extrinsic catalytic sector, CF1. Stimulated by the elucidation of a three‐dimensional partial structure of the mitochondrial enzyme, substantial progress has been made to understand the catalytic mechanism and interesting hypotheses have been proposed about the molecular mechanism of energy coupling. The review discusses the present state of knowledge concerning the structure, molecular genetics, catalytic mechanism, energy coupling and regulation of this important enzyme involved in photophosphorylation.
Key concepts: Photophosphorylation, ATP synthase, Thylakoid, Electrochemical gradient, ATP synthase gamma subunit, Chemiosmosis, Chloroplast, F-ATPase