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R. D. Britt

Researcher at University of California, Berkeley

Publications -  10
Citations -  594

R. D. Britt is an academic researcher from University of California, Berkeley. The author has contributed to research in topics: Extended X-ray absorption fine structure & Electron paramagnetic resonance. The author has an hindex of 9, co-authored 10 publications receiving 585 citations.

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Journal ArticleDOI

Comparison of the structure of the manganese complex in the S1 and S2 states of the photosynthetic O2-evolving complex: an x-ray absorption spectroscopy study.

TL;DR: Results of X-ray K-edge and extendedX-ray absorption fine structure (EXAFS) studies of Mn in the S1 and S2 states of the photosynthetic O2-evolving complex in photosystem II preparations from spinach are presented.
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The S3 state of photosystem II: differences between the structure of the manganese complex in the S2 and S3 states determined by X-ray absorption spectroscopy.

TL;DR: The subtle differences observed between the S states are best explained by an increase in the spread of Mn-Mn distances occurring during the S2----S3 state transition, which suggests the presence of two inequivalent di-mu-oxo-bridged binuclear structures in the S3 state.
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The S0 state of photosystem II induced by hydroxylamine: differences between the structure of the manganese complex in the S0 and S1 states determined by X-ray absorption spectroscopy

TL;DR: It is concluded that, in the presence of hydroxylamine, illumination causes a reduction of the OEC, resulting in a state resembling S0, and a significant structural rearrangement occurs between the S0* and S1 states.
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Characterization of the manganese O2-evolving complex and the iron−quinone acceptor complex in photosystem II from a thermophilic cyanobacterium by electron paramagnetic resonance and X-ray absorption spectroscopy

TL;DR: The striking similarity of these results to those from spinach PS II suggests that the structure of the Mn complex is largely conserved across evolutionarily diverse O2-evolving photosynthetic species.
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The manganese site of the photosynthetic oxygen-evolving complex probed by EPR spectroscopy of oriented photosystem II membranes: the g = 4 and g = 2 multiline signals.

TL;DR: The dramatic NH3-induced changes in the g = 4 signal resolved in the spectra of oriented samples are suggestive that NH3 binding at the Cl- site of the OEC may represent direct coordination of NH3 to the Mn cluster.