Please use this identifier to cite or link to this item: http://ktisis.cut.ac.cy/handle/10488/6662
Title: CO photolysis of cytochrome oxidase investigated by ps resonance Raman spectroscopy
Authors: Schelvis, Johannes
Deinum, Geurt
Varotsis, Constantinos 
Keywords: Cytochrome oxidase
Photochemistry
Raman spectroscopy
Chemistry
Heme
Ligands
Issue Date: 1999
Publisher: Hindawi Publishing Corporation
Source: Laser chemistry, 1999, Volume 19, Issue 1-4, Pages 223-225
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
URI: http://ktisis.cut.ac.cy/handle/10488/6662
ISSN: 02786273
DOI: 10.1155/1999/67252
Rights: © 1999 OPA (Overseas Publishers Association) N.V. Published by license under the Harwood Academic Publishers imprint, part of The Gordon and Breach Publishing Group
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