1. Rotor subunits adaptations in ATP synthases from photosynthetic organisms
- Author
-
Thomas Meier and Anthony Cheuk
- Subjects
Models, Molecular ,Biochemistry & Molecular Biology ,Bioenergetics ,PH ,Protein Conformation ,Protein subunit ,EPSILON-SUBUNIT ,Bacillus ,0601 Biochemistry and Cell Biology ,Photosynthesis ,F0F1-ATP SYNTHASE ,STOICHIOMETRY ,F1Fo-ATP synthase ,Biochemistry ,Oxidative Phosphorylation ,C-RING ,chemistry.chemical_compound ,Adenosine Triphosphate ,Structural Biology ,ATP hydrolysis ,PROTON MOTIVE FORCE ,Spirulina ,F-1-ATPASE ,Review Articles ,Science & Technology ,Bacteria ,ATP synthase ,biology ,DELTA-PSI ,Chemistry ,regulation ,STATE ,Transmembrane protein ,Protein Subunits ,Proton-Translocating ATPases ,1101 Medical Biochemistry and Metabolomics ,Thylakoid ,biology.protein ,Biophysics ,BINDING SITE ,ion-to-ATP ratio ,Life Sciences & Biomedicine ,Adenosine triphosphate ,rotor c-ring - Abstract
Driven by transmembrane electrochemical ion gradients, F-type ATP synthases are the primary source of the universal energy currency, adenosine triphosphate (ATP), throughout all domains of life. The ATP synthase found in the thylakoid membranes of photosynthetic organisms has some unique features not present in other bacterial or mitochondrial systems. Among these is a larger-than-average transmembrane rotor ring and a redox-regulated switch capable of inhibiting ATP hydrolysis activity in the dark by uniquely adapted rotor subunit modifications. Here, we review recent insights into the structure and mechanism of ATP synthases specifically involved in photosynthesis and explore the cellular physiological consequences of these adaptations at short and long time scales.
- Published
- 2021