CO Photolysis of Cytochrome Oxidase Investigated by Ps Resonance Raman Spectroscopy
Document Type
Article
Publication Date
1-1-1999
Abstract
Low-power picosecond resonance Raman spectroscopy was used to investigate the identity of the axial ligand of heme a3 and relaxation processes in the heme a3 pocket of cytochrome oxidase after CO photolysis. Our results show that the proximal histidine remains ligated to heme a3 after CO photolysis excluding the transient ligation of a photolabile, endogenous ligand. Furthermore, the relaxation of the heme a3 macrocycle modes occurs on the sub ps time scale, while relaxation of the heme pocket to its equilibrium conformation takes place on the μs time scale.
DOI
10.1155/1999/67252
Montclair State University Digital Commons Citation
Schelvis, Johannes; Varotsis, Constantinos; Deinum, Geurt; and Babcock, Gerald T., "CO Photolysis of Cytochrome Oxidase Investigated by Ps Resonance Raman Spectroscopy" (1999). Department of Chemistry and Biochemistry Faculty Scholarship and Creative Works. 181.
https://digitalcommons.montclair.edu/chem-biochem-facpubs/181