Effect of high pressure on the photochemical reaction center from Rhodobacter sphaeroides R26.1.
High-pressure studies on the photochemical reaction center from the photosynthetic bacterium Rhodobacter sphaeroides, strain R26.1, shows that, up to 0.6 GPa, this carotenoid-less membrane protein does not loose its three-dimensional structure at room temperature. However, as evidenced by Fourier-transform preresonance Raman and electronic absorption spectra, between the atmospheric pressure and 0.2 GPa, the structure of the bacterial reaction center experiences a number of local reorganizations in the binding site of the primary electron donor. Above that value, the apparent compressibility of this membrane protein is inhomogeneous, being most noticeable in proximity to the bacteriopheophytin molecules. In this elevated pressure range, no more structural reorganization of the primary electron donor binding site can be observed. However, its electronic structure becomes dramatically perturbed, and the oscillator strength of its Q(y) electronic transition drops by nearly one order of magnitude. This effect is likely due to very small, pressure-induced changes in its dimeric structure.
Laboratoire Léon Brillouin, 91191 Gif-sur-Yvette, France. agall@cea.fr
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Gall
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Ellervee
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Bellissent-Funel
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Robert
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Freiberg
D001429:Bacteriochlorophylls / Q000737:chemistry; D001665:Binding Sites; D045342:Light-Harvesting Protein Complexes; D010777:Photochemistry; D010788:Photosynthesis; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry*; D011312:Pressure; D012242:Rhodobacter sphaeroides / Q000378:metabolism*; D013053:Spectrophotometry; D013059:Spectrum Analysis, Raman
D001429:Bacteriochlorophylls; D045342:Light-Harvesting Protein Complexes; D045322:Photosynthetic Reaction Center Complex Proteins