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  • Quantum Electronics and Laser Science Conference
  • OSA Technical Digest (Optica Publishing Group, 1997),
  • paper QThG11

Ultrafast protein solvation dynamics in the α subunit of C-phycocyanin

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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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