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Temporal and spectral characterization of the photosynthetic reaction center from Heliobacterium modesticaldum
Authors:Adrien Chauvet  Josephine Sarrou  Su Lin  Steven P Romberger  John H Golbeck  Sergei Savikhin  Kevin E Redding
Institution:1. Department of Physics, Purdue University, 525 Northwestern Ave, West Lafayette, IN, 47907, USA
2. Department of Chemistry and Biochemistry, Arizona State University, Tempe, AZ, 85287-1604, USA
3. Biodesign Institute, Arizona State University, Tempe, AZ, 85287-1604, USA
4. Department of Biochemistry and Molecular Biology, The Pennsylvania State University, 328 South Frear Laboratory, University Park, PA, 16802, USA
5. Department of Chemistry, The Pennsylvania State University, 328 South Frear Laboratory, University Park, PA, 16802, USA
Abstract:A time-resolved spectroscopic study of the isolated photosynthetic reaction center (RC) from Heliobacterium modesticaldum reveals that thermal equilibration of light excitation among the antenna pigments followed by trapping of excitation and the formation of the charge-separated state P800 +A0 occurs within ~25 ps. This time scale is similar to that reported for plant and cyanobacterial photosystem I (PS I) complexes. Subsequent electron transfer from the primary electron acceptor A0 occurs with a lifetime of ~600 ps, suggesting that the RC of H. modesticaldum is functionally similar to that of Heliobacillus mobilis and Heliobacterium chlorum. The (A0  ? A0) and (P800 + ? P800) absorption difference spectra imply that an 81-OH-Chl a F molecule serves as the primary electron acceptor and occupies the position analogous to ec3 (A0) in PS I, while a monomeric BChl g pigment occupies the position analogous to ec2 (accessory Chl). The presence of an intense photobleaching band at 790 nm in the (A0  ? A0) spectrum suggests that the excitonic coupling between the monomeric accessory BChl g and the 81-OH-Chl a F in the heliobacterial RC is significantly stronger than the excitonic coupling between the equivalent pigments in PS I.
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