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Curr Opin Chem Biol. 2015 Apr;25:152-8. doi: 10.1016/j.cbpa.2014.12.040. Epub 2015 Jan 24.

Oxygen-evolving complex of Photosystem II: an analysis of second-shell residues and hydrogen-bonding networks.

Author information

1
Department of Chemistry, Yale University, New Haven, CT 06520-8107, United States.
2
Department of Chemistry, Yale University, New Haven, CT 06520-8107, United States. Electronic address: gary.brudvig@yale.edu.

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.

PMID:
25621456
DOI:
10.1016/j.cbpa.2014.12.040
[Indexed for MEDLINE]

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