| Literature DB >> 12606050 |
Alberto Mezzetti1, Winfried Leibl, Jacques Breton, Eliane Nabedryk.
Abstract
The photoreduction of the quinone (Q) pool in the photosynthetic membrane of the purple bacterium Rhodobacter sphaeroides was investigated by steady-state and time-resolved Fourier transform infrared difference spectroscopy. The results are consistent with the existence of a homogeneous Q pool inside the chromatophore membrane, with a size of around 20 Q molecules per reaction center. IR marker bands for the quinone/quinol (Q/QH(2)) redox couple were recognized. QH(2) bands are identified at 1491, 1470, 1433 and 1388-1375 cm(-1). The 1491 cm(-1) band, which is sensitive to (1)H/(2)H exchange, is assigned to a C-C ring mode coupled to a C-OH mode. A feature at approximately 1743/1720 cm(-1) is tentatively related to a perturbation of the carbonyl modes of phospholipid head groups induced by QH(2) formation. Complex conformational changes of the protein in the amide I and II spectral ranges are also apparent during reduction and reoxidation of the Q pool.Entities:
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Year: 2003 PMID: 12606050 DOI: 10.1016/s0014-5793(03)00118-2
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124