Reconstitution of H+ translocation and photophosphorylation with photosystem I reaction centers, PMS, and CF“1CF”0

Günter Hauska, Nathan Nelson

Research output: Contribution to journalArticlepeer-review

Abstract

This chapter discusses the reconstitution of H+Translocation and photophosphorylation with photosystem I reaction centers, phenazine methosulfate (PMS), and CF1CF0. With an appropriate artificial redox system such as PMS in the presence of an inhibitor for electron transport from photosystem II, very high rates of photophosphorylation can be achieved. This partial reaction catalyzed by photosystem I constitutes an artificial chemiosmotic loop, because PMS translocates protons from outside to inside the chloroplast thylakoids during its redox cycle that is driven by the light-induced charge separation across the membrane in the reaction center. Light-induced quench of 9-aminoacridine in the presence of reduced PMS indicates the H+uptake into the vesicles. Without the proton pumping by Photosystem I reaction centers (PSI-RC) and PMS, CF1CF0liposomes do not catalyze net ATP synthesis, but carry out uncoupler-sensitive ATP/Piexchange. The chapter outlines the procedures for the preparation of PSI-RC and CF1CF0.

Original languageEnglish
Pages (from-to)285-293
Number of pages9
JournalMethods in Enzymology
Volume126
Issue numberC
DOIs
StatePublished - 1 Jan 1986

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