ATP synthase: Driven and activated by protonmotive force

Autor(en): Hasler, KM
Fritsche, O
Groth, G
Junge, W 
Stichwörter: ADENINE-NUCLEOTIDES; ATP synthesis; BINDING; biophysical chemistry; catalysis; Chemistry; Chemistry, Physical; CHLOROPLAST ATPASE; FIELD; LIGHT; MECHANISM; membranes; PHOSPHORYLATION; PHOTOPHOSPHORYLATION; SPINACH-CHLOROPLASTS; THYLAKOIDS
Erscheinungsdatum: 1996
Herausgeber: VCH PUBLISHERS INC
Journal: BERICHTE DER BUNSEN-GESELLSCHAFT-PHYSICAL CHEMISTRY CHEMICAL PHYSICS
Volumen: 100
Ausgabe: 12
Startseite: 2024
Seitenende: 2027
Zusammenfassung: 
ATP synthase (F-ATPase) of chloroplasts, CF0CF1, is both activated and driven by transmembrane protonmotive force. We dichotomized between activating and driving proton transfer by specific inhibitors, tentoxin and venturicidin. Thylakoid membranes were submitted to voltage steps (by flashing fight) that were superimposed to a steady pH-difference. Transient proton uptake, transfer and release by CF0CF1 were studied by spectroscopic probes. Both, activation and catalysis required all three partial reactions of the proton. A fast electrogenic reaction preceded the catalytic turnover of CF0CF1. This activating electrogenic event in response to the rapid onset of the electric potential is an integral portion of the reaction sequence producing ATP.
Beschreibung: 
95th Annual Meeting of the Deutsche-Bunsen-Gesellschaft-fur-Physikalische-Chemie on Primary Processes of Photosynthesis, JENA, GERMANY, MAY 16-18, 1996
ISSN: 00059021

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