CO photolysis of cytochrome oxidase investigated by ps resonance Raman spectroscopy

Johannes Schelvis, Costas Varotsis, Geurt Deinum, Gerald T. Babcock

Research output: Contribution to journalArticle

1 Citation (Scopus)

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.

Original languageEnglish
Pages (from-to)223-225
Number of pages3
JournalLaser Chemistry
Volume19
Issue number1-4
DOIs
StatePublished - 1 Jan 1999

Fingerprint

Raman Spectrum Analysis
Photolysis
oxidase
cytochromes
Electron Transport Complex IV
Carbon Monoxide
photolysis
Raman spectroscopy
ligands
histidine
Ligands
Relaxation processes
Heme
Histidine
Ligation
Conformations
heme a

Keywords

  • CO
  • Cytochrome oxidase
  • Photolysis
  • Picosecond
  • Resonance Raman

Cite this

Schelvis, Johannes ; Varotsis, Costas ; Deinum, Geurt ; Babcock, Gerald T. / CO photolysis of cytochrome oxidase investigated by ps resonance Raman spectroscopy. In: Laser Chemistry. 1999 ; Vol. 19, No. 1-4. pp. 223-225.
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CO photolysis of cytochrome oxidase investigated by ps resonance Raman spectroscopy. / Schelvis, Johannes; Varotsis, Costas; Deinum, Geurt; Babcock, Gerald T.

In: Laser Chemistry, Vol. 19, No. 1-4, 01.01.1999, p. 223-225.

Research output: Contribution to journalArticle

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