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

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 microsecond-20 msec at room temperature. No detectable change in the protein fluorescence intensity...

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Pubblicato in:Proc Natl Acad Sci U S A
Autori principali: Fukumoto, J M, Hopewell, W D, Karvaly, B, El-Sayed, M A
Natura: Artigo
Lingua:Inglês
Pubblicazione: National Academy of Sciences 1981
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Accesso online:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC319030/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/6941246/
https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.78.1.252
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