Abstract
We have performed a series of femtosecond transient hole-burning studies with a range of pump wavelengths on the α. subunit of the cyanobacterial light-harvesting protein C-phycocyanin to understand how the protein matrix controls the excited-state potential surfaces of hound chromophores. The α subunit contains a single phycocyanobilin (open-chain tetrapyrrole) chromophore bound via a cysteine-derived thioether linkage. The studies were performed with the α subunit in both H2O and after the hydrogens have been exchanged with deuterium in D2O
© 1997 Optical Society of America
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