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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1994 Jan 18;91(2):704–708. doi: 10.1073/pnas.91.2.704

Identification of histidine at the catalytic site of the photosynthetic oxygen-evolving complex.

X S Tang 1, B A Diner 1, B S Larsen 1, M L Gilchrist Jr 1, G A Lorigan 1, R D Britt 1
PMCID: PMC43017  PMID: 8290585

Abstract

The molecular oxygen in our atmosphere is a product of a water-splitting reaction that occurs in the oxygen-evolving complex of photosystem II of oxygenic photosynthesis. The catalytic core of the oxygen-evolving complex is an ensemble of four manganese atoms arranged in a cluster of undetermined structure. The pulsed electron paramagnetic resonance (EPR) technique of electron spin-echo envelope modulation (ESEEM) can be used to measure nuclear spin transitions of nuclei magnetically coupled to paramagnetic metal centers of enzymes. We report the results of ESEEM experiments on the cyanobacterium Synechocystis PCC 6803 selectively labeled with 15N at the two nitrogen sites of the imidazole side chain of histidine residues. The experiments demonstrate that histidine is bound to manganese in the oxygen-evolving complex.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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