Chlorophyll a Dimers Bound in the Water-Soluble Protein BoWSCP Photosensitize the Reduction of Cytochrome c.
WSCP proteins
chlorophyll a dimer
cytochrome c
photochemistry
tris(hydroxymethyl)aminomethane
Journal
Doklady. Biochemistry and biophysics
ISSN: 1608-3091
Titre abrégé: Dokl Biochem Biophys
Pays: United States
ID NLM: 101126895
Informations de publication
Date de publication:
Apr 2023
Apr 2023
Historique:
received:
24
10
2022
accepted:
30
11
2022
revised:
20
11
2022
medline:
22
6
2023
pubmed:
21
6
2023
entrez:
20
6
2023
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 37340294
doi: 10.1134/S1607672923700126
pii: 10.1134/S1607672923700126
doi:
Substances chimiques
Chlorophyll A
YF5Q9EJC8Y
Cytochromes c
9007-43-6
Water
059QF0KO0R
Chlorophyll
1406-65-1
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
60-64Informations de copyright
© 2023. Pleiades Publishing, Ltd.
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