Generation of Photoelectric Responses by Photosystem II Core Complexes in the Presence of Externally Added Cytochrome c. 2021

Liya A Vitukhnovskaya, and Ruben A Simonyan, and Alexey Yu Semenov, and Mahir D Mamedov
Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, 119992, Russia.

The effect of exogenous cytochrome c (cyt c) on kinetics of photoelectric responses (Δψ) of two types of photosystem II (PSII) core complexes (intact - PSII with active water-oxidizing complex and Mn-depleted complex) reconstituted into liposomes has been investigated by direct electrometric technique. PSII complexes were localized in the proteoliposome membranes with their donor side outward. An additional electrogenic phase was observed in the kinetics of Δψ generation in response to a laser flash besides the main fast (<0.3 µs) electrogenic component due to electron transfer from the redox-active tyrosine YZ to the primary quinone acceptor QA in the presence of oxidized cyt c (cyt c3+) entrapped in the internal space of proteoliposomes with intact PSII complexes. This component with characteristic time τ ≈ 40 µs and relative amplitude of ~10% of the total Δψ was attributed to the vectorial electron transfer from QA- to cyt c3+ serving as an external acceptor. An additional electrogenic component with τ ~ 70 µs and a relative amplitude of ~20% of the total Δψ also appeared in the kinetics of Δψ formation, when cyt c2+ was added to the suspension of proteoliposomes containing Mn-depleted PSII core complexes. This component was attributed to the electrogenic transfer of an electron from cyt c2+ to photooxidized tyrosine YZ. These data imply that cyt c3+ serves as a very effective exogenous electron acceptor for QA- in the case of intact PSII core complexes, and cyt c2+ is an extremely efficient artificial electron donor for YZ in the Mn-depleted PSII. The obtained data on the roles of cyt c2+ and cyt c3+ as an electron donor and acceptor for PSII, respectively, can be used to develop hybrid photoelectrochemical solar energy-converting systems based on photosynthetic pigment-protein complexes.

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
D004579 Electron Transport The process by which ELECTRONS are transported from a reduced substrate to molecular OXYGEN. (From Bennington, Saunders Dictionary and Encyclopedia of Laboratory Medicine and Technology, 1984, p270) Respiratory Chain,Chain, Respiratory,Chains, Respiratory,Respiratory Chains,Transport, Electron
D045304 Cytochromes c Cytochromes of the c type that are found in eukaryotic MITOCHONDRIA. They serve as redox intermediates that accept electrons from MITOCHONDRIAL ELECTRON TRANSPORT COMPLEX III and transfer them to MITOCHONDRIAL ELECTRON TRANSPORT COMPLEX IV. Cytochrome c,Ferricytochrome c,Ferrocytochrome c,Apocytochrome C
D045332 Photosystem II Protein Complex A large multisubunit protein complex found in the THYLAKOID MEMBRANE. It uses light energy derived from LIGHT-HARVESTING PROTEIN COMPLEXES to catalyze the splitting of WATER into DIOXYGEN and of reducing equivalents of HYDROGEN. Chloroplast Reaction Center Protein D1,D1 Photosystem II Protein, Plant,Light-Induced D1 Protein, Photosystem II,Oxygen Evolving Enzyme,PRCP II D2 Protein,Photosystem II,Photosystem II Reaction Center,Photosystem II Reaction Center Complex D1 Protein,Photosystem II Reaction Center Complex D2 Protein,RCII-D1 Protein,Water Oxidase,Water-Splitting Enzyme of Photosynthesis,Enzyme, Oxygen Evolving,Evolving Enzyme, Oxygen,Light Induced D1 Protein, Photosystem II,Oxidase, Water,Photosynthesis Water-Splitting Enzyme,Water Splitting Enzyme of Photosynthesis
D018724 Spinacia oleracea A widely cultivated plant, native to Asia, having succulent, edible leaves eaten as a vegetable. (From American Heritage Dictionary, 1982) Spinach

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