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Article

Mutagenesis of CP43-arginine-357 to serine reveals new evidence for (bi)carbonate functioning in the water oxidizing complex of Photosystem II.

Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology - 1 Dec 2005

Ananyev Gennady, Nguyen Tuan, Putnam-Evans Cindy, Dismukes G Charles

Abstract excerpt

The chlorophyll-binding protein CP43 is an inner subunit of the Photosystem II (PSII) reaction center core complex of all oxygenic photoautotrophs. X-Ray structural evidence places the guanidinium cation of the conserved arginine 357 residue of CP43 within a few Angstroms to the Mn(4)Ca cluster of the water-oxidizing complex (WOC) and has been implicated as a possible carbonate binding site. To test the...

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Identifiers

PMID: 16307112
DOI: 10.1039/b507519j

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Mutagenesis of CP43-arginine-357 to serine reveals new evidence for (bi)carbonate functioning in the water oxidizing complex of Photosystem II.PMID 16307112Read ↗

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