A protein conformational change associated with the photoreduction of the primary and secondary quinones in the bacterial reaction center
- 18 June 1990
- journal article
- Published by Wiley in FEBS Letters
- Vol. 266 (1-2) , 59-62
- https://doi.org/10.1016/0014-5793(90)81506-j
Abstract
A comparison is made between the PQA → P+Q−A and PQAQB → P+QAQ−B transitions in Rps. viridis and Rb. sphaeroides reaction centers (RCs) by the use of light-induced Fourier transform infrared (FTIR) difference spectroscopy. In Rb. sphaeroides RCs, we identify a signal at 1650 cm−1 which is present in the P+QA-minus-PQA spectrum and not in the P+QAQ−B-minus-PQAQB spectrum. In contrast, this signal is present in both P+Q−A-minus-PQ−A and P+QAQ−B-minus-PQAQB spectra of Rps. viridis RCs. These data are interpreted in terms of a conformational change of the protein backbone near QA (possible at the peptide CO of a conserved alanine residue in the QA pocket) and of the different bonding interactions of QB with the protein in the RC of the two speciesKeywords
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