Identification of Histidine at the Catalytic Site of the Photosynthetic Oxygen-Evolving Complex

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 st...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1994-01, Vol.91 (2), p.704-708
Main Authors: Tang, Xiao-Song, Diner, Bruce A., Larsen, Barbara S., Gilchrist, M. Lane, Lorigan, Gary A., Britt, R. David
Format: Article
Language:English
Subjects:
Amino acids
Binding Sites
Biological and medical sciences
Biology
Cell structures and functions
Chloroplast, photosynthetic membrane and photosynthesis
Cyanobacteria - metabolism
Electron Spin Resonance Spectroscopy
Electrons
Fundamental and applied biological sciences. Psychology
Histidine - chemistry
Imidazoles
Ligands
Magnetic fields
Manganese
Manganese - chemistry
Molecular and cellular biology
Nitrogen
Oxygen
Oxygen - metabolism
Oxygen evolving complex
Photosynthesis - physiology
Photosynthetic Reaction Center Complex Proteins - chemistry
Photosynthetic Reaction Center Complex Proteins - metabolism
Protons
Synechocystis
Thylakoids
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Summary: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 with15N 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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.91.2.704