FEBS Letters | |
Time‐resolved tryptophan fluorescence in photosynthetic reaction centers from Rhodobacter sphaeroides | |
Blankenship, Robert E.2  Causgrove, Timothy P.2  Godik, Valentina I.1  Woodbury, Niel2  | |
[1] A.N. Belozersky Institute of Physico-Chemical Biology of Moscow State University, Moscow 119899, Russian Federation;Department of Chemistry and Biochemistry, Center for the Study of Early Events in Photosynthesis, Arizona State University, Tempe, AZ 85287-1604, USA | |
关键词: Reaction center; Tryptophan; Stationary and time-resolved fluorescence; Protein conformation; Rhodobacter sphaeroides; BChl; bacteriochlorophyll; BPh; bacteriopheophytin; FWHM; full-width at half-maximum; Trp; tryptophan; Q−; reduced quinone; DAS; decay associated emission spectra; P+; photooxidized bacteriochlorophyll special pair; χ2; chi-square; | |
DOI : 10.1016/0014-5793(93)80114-A | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Tryptophan fluorescence of reaction centers isolated from Rhodobacter sphaeroides, both stationary and time-resolved, was studied. Fluorescence kinetics were found to fit best a sum of four discrete exponential components. Half of the initial amplitude was due to a component with a lifetime of ≅ 60 ps, belonging to Trp residues, capable of efficient transfer of excitation energy to bacteriochlorophyll molecules of the reaction center. The three other components seem to be emitted by Trp ground-state conformers, unable to participate in such a transfer. Under the influence of intense actinic light, photooxidizing the reaction centers, the yield of stationary fluorescence diminished by ⋍1.5 times, while the number of the kinetic components and their life times remained practically unchanged. Possible implications of the observed effects for the primary photosynthesis events are considered.
【 授权许可】
Unknown
【 预 览 】
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