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Title: Time-resolved protein fluorescence studies of intermediates in the photochemical cycle of bacteriorhodopsin

Journal Article · · Proc. Natl. Acad. Sci. U.S.A.; (United States)

The photolysis-induced changes in the protein fluorescence intensity(at 320 nm) during the proton-pumping cycle of bacteriorhodopsin were examined by a delayed two-pulse technique in the time range 1 ..mu..sec-20 msec at room temperature. No detectable change in the protein fluorescence intensity was observed on the earliest time scale within the lifetime of the intermediate K/sub 590/, when retinal apparently undergoes the largest structural changes. The time dependence of the relative changes in fluorescence intensity did, however, display a close correlation with the population of L/sub 550/ and M/sub 412/ intermediates. From a computer numerical fit of the data, with available published kinetic parameters, the protein fluorescence quantum yields of the K/sub 590/, L/sub 550/, and M/sub 412/ intermediates are found to be 1.0, 0.92, and 0.80 of that for native bR/sub 570/, respectively. The probable mechanisms of the observed fluorescence quenching during the photochemical cycle are qualitatively discussed.

Research Organization:
Univ. of California, Los Angeles, CA (United States)
OSTI ID:
6579676
Journal Information:
Proc. Natl. Acad. Sci. U.S.A.; (United States), Vol. 78:1
Country of Publication:
United States
Language:
English