Chlorophyll a Dimers Bound in the Water-Soluble Protein BoWSCP Photosensitize the Reduction of Cytochrome c
When bound to water-soluble proteins of the WSCP family, chlorophyll molecules form dimers structurally similar to the “special pair” of chlorophylls (bacteriochlorophylls) in photosynthetic reaction centers. Being exposed to red light (λ ≥ 650 nm) in oxygen-free solutions, chlorophyll a dimers harb...
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Veröffentlicht in: | Doklady. Biochemistry and biophysics 2023-04, Vol.509 (1), p.60-64 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | When bound to water-soluble proteins of the WSCP family, chlorophyll molecules form dimers structurally similar to the “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
. |
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ISSN: | 1607-6729 1608-3091 |
DOI: | 10.1134/S1607672923700126 |