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Open AccessJournal ArticleDOI

ESR, ENDOR and TRIPLE resonance studies of the primary donor radical cation P960+• in the photosynthetic bacterium Rhodopseudomonas viridis

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TLDR
In this article, the light-induced radical cation of the primary electron donor P960+• in photosynthetic reaction centers from Rhodopseudomonas viridis has been investigated by ESR, ENDOR and TRIPLE techniques.
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This article is published in Chemical Physics Letters.The article was published on 1988-07-22 and is currently open access. It has received 58 citations till now. The article focuses on the topics: Unpaired electron & Photosynthetic reaction centre.

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Journal ArticleDOI

Photophysics of photosynthesis. Structure and spectroscopy of reaction centers of purple bacteria

TL;DR: In this article, a detailed account of investigations on the functioning of the reaction center protein with a number of optical and magnetic resonance spectroscopic techniques is presented, with emphasis on the relation between structure and function.
Journal ArticleDOI

Electrostatic control of charge separation in bacterial photosynthesis.

TL;DR: Electrostatic interaction energies of the electron carriers with their surroundings in a photosynthetic bacterial reaction center are calculated and are shown to be relatively insensitive to various details of the model, including the charge distribution in P+, the atomic charges used for the amino acid residues, the boundaries of the structural region that is considered microscopically and the treatments of the histidyl ligands of P and of potentially ionizable amino acids.
Journal ArticleDOI

The electronic structure of the primary donor cation radical in Rhodobacter sphaeroides R-26: ENDOR and TRIPLE resonance studies in single crystals of reaction centers

TL;DR: The electron spin density distribution of the cation radical of the primary donor, D+, a bacteriochlorophyll a dimer was determined by endor and TRIPLE resonance experiments performed on single crystals of reaction centers (RCs) of Rhodobacter sphaeroides R-26 as mentioned in this paper.
Book ChapterDOI

The Pathway, Kinetics and Thermodynamics of Electron Transfer in Wild Type and Mutant Reaction Centers of Purple Nonsulfur Bacteria

TL;DR: In this article, the electron transfer reactions of purple nonsulfur bacteria such as Rhodobacter sphaeroides have been characterized on the timescale of the actual reactions, with the first of them taking place within a few picoseconds.
Journal ArticleDOI

ENDOR and special triple resonance studies of chlorophyll cation radicals in photosystem 2.

TL;DR: Electron nuclear double resonance (ENDOR) and special triple resonance spectroscopies have been used to study the cation radicals of the primary donor, P680, and two secondary donor chlorophylls in photosystem 2 (PS2), suggesting that P680.+ is a weakly coupled chlorophyLL pair with 82% of the unpaired electron spin located on one chlorophylla of the pair at 15 K.
References
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Journal ArticleDOI

Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3Å resolution

TL;DR: The molecular structure of the photosynthetic reaction centre from Rhodopseudomonas viridis has been elucidated using X-ray crystallographic analysis and the first description of the high-resolution structure of an integral membrane protein is presented.
Journal ArticleDOI

X-ray structure analysis of a membrane protein complex. Electron density map at 3 Å resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis

TL;DR: In this paper, an atomic model of the prosthetic groups of the reaction center complex (4 bacteriochlorophyll b, 2 bacteriopheophytin b, 1 non-heme iron, 1 menaquinone, 4 heme groups) was built.
Book

Biological Magnetic Resonance

TL;DR: Volume 9 of the highly successful series of topical, authoritative chapters on new aspects of biological magnetic resonance is presented, ranging from applications of in vivo magnetic resonance to more fundamental aspects of electron spin resonance and nuclear magnetic resonance.
Journal ArticleDOI

A simple procedure for removal of Triton X-100 from protein samples.

TL;DR: A simple procedure is described for removal of Triton X-100 from protein samples by adsorption of the detergent on a commercial copolymer in bead form with no loss or dilution of protein.
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