[High-order derivative spectroscopy of infrared absorption spectra of the reaction centers from Rhodobacter sphaeroides].
The infrared absorption spectra of reduced and chemically oxidized reaction center preparations from the purple bacterium Rhodobacter sphaeroides were investigated by means of high-order derivative spectroscopy. The model Gaussian band with a maximum at 810 nm and a half-band of 15 nm found in the absorption spectrum of the reduced reaction center preparation is eliminated after the oxidation of photoactive bacteriochlorophyll dimer (P). This band was related to the absorption of the P(+)y excitonic band of P. On the basis of experimental results, it was concluded that the bleaching of the P(+)y absorption band at 810 nm in the oxidized reaction center preparations gives the main contribution to the blue shift of the 800 nm absorption band of Rb. sphaeroides reaction centers.
D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D001429:Bacteriochlorophylls / Q000737:chemistry* / Q000378:metabolism; D010084:Oxidation-Reduction; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry* / Q000378:metabolism; D012242:Rhodobacter sphaeroides / Q000201:enzymology*; D013055:Spectrophotometry, Infrared
D001426:Bacterial Proteins; D001429:Bacteriochlorophylls; D045322:Photosynthetic Reaction Center Complex Proteins