Literature DB >> 10675555

X-ray crystal structure of the YM210W mutant reaction centre from Rhodobacter sphaeroides.

K E McAuley1, P K Fyfe, R J Cogdell, N W Isaacs, M R Jones.   

Abstract

The X-ray crystal structure of a reaction centre from Rhodobacter sphaeroides with a mutation of tyrosine M210 to tryptophan (YM210W) has been determined to a resolution of 2.5 A. Structural conservation is very good throughout the body of the protein, with the tryptophan side chain adopting a position in the mutant complex closely resembling that of the tyrosine in the wild-type complex. The spectroscopic properties of the YM210W reaction centre are discussed with reference to the structural data, with particular focus on evidence that the introduction of the bulkier tryptophan in place of the native tyrosine may cause a small tilt of the macrocycle of the B(L) monomeric bacteriochlorophyll.

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Year:  2000        PMID: 10675555     DOI: 10.1016/s0014-5793(00)01172-8

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  6 in total

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Journal:  Photosynth Res       Date:  2014-09-21       Impact factor: 3.573

4.  Dynamics of diverse coherences in primary charge separation of bacterial reaction center at 77 K revealed by wavelet analysis.

Authors:  Fei Ma; Elisabet Romero; Michael R Jones; Vladimir I Novoderezhkin; Long-Jiang Yu; Rienk van Grondelle
Journal:  Photosynth Res       Date:  2021-10-28       Impact factor: 3.573

5.  Putative hydrogen bond to tyrosine M208 in photosynthetic reaction centers from Rhodobacter capsulatus significantly slows primary charge separation.

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6.  Both electronic and vibrational coherences are involved in primary electron transfer in bacterial reaction center.

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  6 in total

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