CHLOROPHYLL  A  DIMERS HARBORED BY WATER-SOLUBLE PROTEIN BoWSCP PHOTOSENSITIZE REDUCTION OF CYTOCHROME  C

Yu. N. Obukhov; Обухов Ю. Н.; K. V. Neverov; Неверов К. В.; Yu. V. Maleeva; Малеева Ю. В.; M. S. Kritsky; Крицкий М. С.

doi:10.31857/S2686738922600790

CHLOROPHYLL A DIMERS HARBORED BY WATER-SOLUBLE PROTEIN BoWSCP PHOTOSENSITIZE REDUCTION OF CYTOCHROME C

Authors: Obukhov Y.N.¹, Neverov K.V.¹, Maleeva Y.V.², Kritsky M.S.¹
Affiliations:
1. Bach Institute of Biochemistry, Federal Research Centre “Fundamentals of Biotechnology” of the Russian Academy of Sciences
2. Faculty of Biology, Moscow State University
Issue: Vol 509, No 1 (2023)
Pages: 191-195
Section: Articles
URL: https://journals.rcsi.science/2686-7389/article/view/135656
DOI: https://doi.org/10.31857/S2686738922600790
EDN: https://elibrary.ru/LZAHVX
ID: 135656

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Abstract
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Abstract

When bound to water-soluble proteins of the WSCP family, chlorophyll molecules form dimers structurally similar to “special pair” of chlorophylls (bacteriochlorophylls) in photosynthetic reaction centers. Being exposed to red light (λ ≥ 650 nm) in oxygen-free solutions, chlorophyll a dimers harbored by BoWSCP holoproteins (from Brassica oleracea var. botrytis) have sensitized the reduction of cytochrome c. According to absorption and circular dichroism spectroscopy data, the photochemical process did not significantly impair the structure of chlorophyll a molecules as well as their dimers harbored by BoWSCP protein. Adding tris(hydroxymethyl)aminomethane as an electron donor for chlorophyll recovery stimulated the photoreduction of cytochrome c.

Keywords

WSCP proteins, chlorophyll a dimer, cytochrome c, photochemistry, tris(hydroxymethyl)aminomethane

References

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