Oxygen-evolving complex of Photosystem II

an analysis of second-shell residues and hydrogen-bonding networks

Leslie Vogt, David J. Vinyard, Sahr Khan, Gary W. Brudvig

Research output: Contribution to journalArticle

Abstract

The oxygen-evolving complex (OEC) is a Mn4O5Ca cluster embedded in the Photosystem II (PSII) protein complex. As the site of water oxidation, the OEC is connected to the lumen by channels that conduct water, oxygen, and/or protons during the catalytic cycle. The hydrogen-bond networks found in these channels also serve to stabilize the oxidized intermediates, known as the S states. We review recent developments in characterizing these networks via protein mutations, molecular inhibitors, and computational modeling. On the basis of these results, we highlight regions of the PSII protein in which changes have indirect effects on the S1, S2, and S3 oxidation states of the OEC while still allowing photosynthetic activity.

Original languageEnglish
Pages (from-to)152-158
Number of pages7
JournalCurrent Opinion in Chemical Biology
Volume25
DOIs
Publication statusPublished - Apr 1 2015

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Photosystem II Protein Complex
Hydrogen Bonding
Hydrogen bonds
Oxygen
Oxidation
Aquaporins
Protons
Hydrogen
Proteins
Mutation
Water

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Oxygen-evolving complex of Photosystem II : an analysis of second-shell residues and hydrogen-bonding networks. / Vogt, Leslie; Vinyard, David J.; Khan, Sahr; Brudvig, Gary W.

In: Current Opinion in Chemical Biology, Vol. 25, 01.04.2015, p. 152-158.

Research output: Contribution to journalArticle

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