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Literature summary for 1.10.3.9 extracted from

  • Kaminskaya, O.P.; Shuvalov, V.A.
    Towards an understanding of redox heterogeneity of the photosystem II cytochrome b559 in the native membrane (2016), Eur. Biophys. J., 45, 129-138 .
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
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Beta vulgaris 16020
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Organism

Organism UniProt Comment Textmining
Beta vulgaris
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
leaf
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Beta vulgaris
-

General Information

General Information Comment Organism
physiological function redox heterogeneity of the native population of Cyt b559 is due to heme-quinone redox interactions. The interacting plastoquinone is caged in the protein interior in the singly protonated state. The model of redox interaction successfully explains the singularity of Cyt b559 among heme proteins, its redox heterogeneity, the atypically high Em value of the high potential form, the large difference in the Em values between the redox forms, and the instability of the heme protein towards mild treatments Beta vulgaris