Heme-CO Religation in Photolyzed Hemoglobin: A Time-Resolved Raman Study of the Fe-CO Stretching Mode

M. C. Schneebeck, L. E. Vigil, J. M. Friedman, M. D. Chavez, M. R. Ondrias

Research output: Contribution to journalArticle

11 Scopus citations

Abstract

Time-resolved resonance Raman spectroscopy has been employed to monitor geminate heme-CO rebinding in photolyzed HbCO. The excitation frequency was tuned to enhance the scattering from rebound heme sites 20–500 ns subsequent to CO photolysis. The behavior of vFe-C during ligand rebinding has important ramifications concerning heme pocket dynamics of the distinct equilibrium configurations of the six-coordinate heme sites. During the geminate phase of recombination, the Fe-CO bond strengths and configurations of the rebound sites (inferred from the positions and line widths of vFc-C) were found to be the same as those of equilibrium configurations of HbCO within 500 ns of CO photolysis for all samples. No evidence was found for the existence of transient metastable configurations during geminate recombination. Spectra obtained at earlier times (100 ns) revealed small differences in the geminate rebinding rates of the two equilibrium configurations. Since there is little or no further CO rebinding between 100 and 500 ns after photolysis, some interconversion must occur between the dominant HbCO configurations on a submicrosecond time scale.

Original languageEnglish (US)
Pages (from-to)1318-1323
Number of pages6
JournalBiochemistry
Volume32
Issue number5
DOIs
StatePublished - Jan 1 1993

ASJC Scopus subject areas

  • Biochemistry

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