Protein-Matrix Solvation Dynamics in the α Subunit of C-Phycocyanin

We have used femtosecond transient hole-burning (THB) spectroscopy to study single-chromophore dynamics at room temperature in the α subunit of C-phycocyanin, a cyanobacterial light-harvesting protein. The α subunit contains a single phycocyanobilin (open-chain tetrapyrrole) chromophore. A reasonabl...

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Bibliographic Details
Published in:Journal of physical chemistry (1952) 1996-08, Vol.100 (33), p.14198-14205
Main Authors: Riter, Ruth R, Edington, Maurice D, Beck, Warren F
Format: Article
Language:English
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Summary:We have used femtosecond transient hole-burning (THB) spectroscopy to study single-chromophore dynamics at room temperature in the α subunit of C-phycocyanin, a cyanobacterial light-harvesting protein. The α subunit contains a single phycocyanobilin (open-chain tetrapyrrole) chromophore. A reasonable description of the THB spectra requires the presence of a broad excited-state absorption (ESA) line shape underlying the entire photobleaching/stimulated emission (PB/SE) region. The time evolution of the THB spectrum involves line broadening on the 100−200-fs time scale and a
ISSN:0022-3654
1541-5740
DOI:10.1021/jp960453j