Handbook of Metalloproteins 2004
DOI: 10.1002/0470028637.met110
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Photosynthetic Reaction Centers of Purple Bacteria

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Cited by 5 publications
(8 citation statements)
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“…The Q B site is formed primarily by residues located on transmembrane helices D (L171-L198) and E (L226-L249) as well as on the intervening cytoplasmic de helix (L209-L220) and the dee loop (L220-L226). 21,22 In addition, the Q B site is delimited against the membrane by the atoms of two cofactors, the phytyl Figure 1. Stigmatellin-binding sites in the cytochrome bc 1 complex (left) and the photosynthetic RC (right).…”
Section: Introductionmentioning
confidence: 99%
“…The Q B site is formed primarily by residues located on transmembrane helices D (L171-L198) and E (L226-L249) as well as on the intervening cytoplasmic de helix (L209-L220) and the dee loop (L220-L226). 21,22 In addition, the Q B site is delimited against the membrane by the atoms of two cofactors, the phytyl Figure 1. Stigmatellin-binding sites in the cytochrome bc 1 complex (left) and the photosynthetic RC (right).…”
Section: Introductionmentioning
confidence: 99%
“…According to the current knowledge, the mutual distances and orientations of the pigments are specifically controlled by the surrounding protein [2]. For the last decades a good deal of data on protein‐cofactor interactions in photosynthetic RCs was accumulated by means of site‐directed mutagenesis [3].…”
Section: Introductionmentioning
confidence: 99%
“…Several different positions of neutral Q B have been found in RC crystal structures [42][43][44][45][46][47][48][49]. Time-resolved crystallographic experiments indicate predominant binding of Q B in the proximal position in both the neutral and charge-separated states and no large motion associated with Q B was observed after the flash on the timescale of secondary electron transfer [50,51].…”
Section: Hydrogen Bondsmentioning
confidence: 99%
“…The location of quinones in quinone-binding proteins, including bacterial RCs [44], Photosystem I [62], Photosystem II [63], and bc 1 complex [64], has been determined in many crystal structures. In all known structures, the quinone headgroup is oriented towards the membrane surface, while the tail is exposed to the membrane dielectric (Fig.…”
Section: Ubiquinone Location In the Proteinsmentioning
confidence: 99%
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