Heme-CO religation in photolyzed hemoglobin: a time-resolved raman study of the Fe-CO stretching mode

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

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

Time-resolved resonance Raman spectroscopy has been employed to monitor geminate hemeCO 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 vFe-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
StatePublished - 1993

Fingerprint

Carbon Monoxide
Heme
Stretching
Photolysis
Hemoglobins
Genetic Recombination
Raman Spectrum Analysis
Linewidth
Raman spectroscopy
Scattering
Ligands

ASJC Scopus subject areas

  • Biochemistry

Cite this

Schneebeck, M. C., Vigil, L. E., Friedman, J. M., Chavez, M. D., & Ondrias, M. R. (1993). Heme-CO religation in photolyzed hemoglobin: a time-resolved raman study of the Fe-CO stretching mode. Biochemistry®, 32(5), 1318-1323.

Heme-CO religation in photolyzed hemoglobin : a time-resolved raman study of the Fe-CO stretching mode. / Schneebeck, M. C.; Vigil, L. E.; Friedman, Joel M.; Chavez, M. D.; Ondrias, M. R.

In: Biochemistry®, Vol. 32, No. 5, 1993, p. 1318-1323.

Research output: Contribution to journalArticle

Schneebeck, MC, Vigil, LE, Friedman, JM, Chavez, MD & Ondrias, MR 1993, 'Heme-CO religation in photolyzed hemoglobin: a time-resolved raman study of the Fe-CO stretching mode', Biochemistry®, vol. 32, no. 5, pp. 1318-1323.
Schneebeck, M. C. ; Vigil, L. E. ; Friedman, Joel M. ; Chavez, M. D. ; Ondrias, M. R. / Heme-CO religation in photolyzed hemoglobin : a time-resolved raman study of the Fe-CO stretching mode. In: Biochemistry®. 1993 ; Vol. 32, No. 5. pp. 1318-1323.
@article{4ca5d4260ada47429903bfa1678df759,
title = "Heme-CO religation in photolyzed hemoglobin: a time-resolved raman study of the Fe-CO stretching mode",
abstract = "Time-resolved resonance Raman spectroscopy has been employed to monitor geminate hemeCO 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 vFe-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.",
author = "Schneebeck, {M. C.} and Vigil, {L. E.} and Friedman, {Joel M.} and Chavez, {M. D.} and Ondrias, {M. R.}",
year = "1993",
language = "English (US)",
volume = "32",
pages = "1318--1323",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "5",

}

TY - JOUR

T1 - Heme-CO religation in photolyzed hemoglobin

T2 - a time-resolved raman study of the Fe-CO stretching mode

AU - Schneebeck, M. C.

AU - Vigil, L. E.

AU - Friedman, Joel M.

AU - Chavez, M. D.

AU - Ondrias, M. R.

PY - 1993

Y1 - 1993

N2 - Time-resolved resonance Raman spectroscopy has been employed to monitor geminate hemeCO 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 vFe-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.

AB - Time-resolved resonance Raman spectroscopy has been employed to monitor geminate hemeCO 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 vFe-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.

UR - http://www.scopus.com/inward/record.url?scp=0027532319&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027532319&partnerID=8YFLogxK

M3 - Article

C2 - 8448140

AN - SCOPUS:0027532319

VL - 32

SP - 1318

EP - 1323

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 5

ER -