Interspecies variations in the transient heme species generated subsequent to CO photolysis from hemoglobins

S. D. Carson, C. A. Wells, E. W. Findsen, Joel M. Friedman, M. R. Ondrias

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

The structure, ligand binding kinetics, and thermodynamics of hemoglobin have been the subject of a great deal of investigation. However, the exact pathway(s) by which cooperative energetics are communicated within the protein remain undefined. The effects of interspecies variations in quaternary and tertiary structure, oxygen affinity, cooperativity, and ligand binding kinetics upon the overall ligand binding process are, therefore, of great importance in understanding and solving these problems. The demonstrated sensitivity of resonance Raman spectroscopy to heme structure and environment make it an ideal probe of ligand binding dynamics. It is possible to examine how specific vibrational modes change with time and correlate this with solution conditions and protein structural and conformational differences. Those modes which exhibit the greatest change with ligand photolysis are also indicative of possible paths of cooperative energy dissipation within the protein. The changes which occur in the vibrational modes of the heme within 10 ns of CO photolysis have been determined for a wide variety of mammalian and reptilian hemoglobins. The modes most affected by this process are, without exception, v(Fe-His), v4, and the substituent bending modes, δ(c(b) - s) and δ(c(b) - c(α) - c(β)). Furthermore, a direct correlation exists between the shift in porphyrin π* electron density upon CO photolysis (as indicated by the transient changes in v4) and the Hill coefficient of cooperativity. The implications of those results concerning ligand binding cooperativity in hemoglobins are discussed.

Original languageEnglish (US)
Pages (from-to)3044-3051
Number of pages8
JournalJournal of Biological Chemistry
Volume262
Issue number7
StatePublished - 1987
Externally publishedYes

Fingerprint

Photolysis
Carbon Monoxide
Heme
Hemoglobins
Ligands
Proteins
Kinetics
Raman Spectrum Analysis
Porphyrins
Thermodynamics
Carrier concentration
Raman spectroscopy
Energy dissipation
Electrons
Oxygen

ASJC Scopus subject areas

  • Biochemistry

Cite this

Interspecies variations in the transient heme species generated subsequent to CO photolysis from hemoglobins. / Carson, S. D.; Wells, C. A.; Findsen, E. W.; Friedman, Joel M.; Ondrias, M. R.

In: Journal of Biological Chemistry, Vol. 262, No. 7, 1987, p. 3044-3051.

Research output: Contribution to journalArticle

Carson, S. D. ; Wells, C. A. ; Findsen, E. W. ; Friedman, Joel M. ; Ondrias, M. R. / Interspecies variations in the transient heme species generated subsequent to CO photolysis from hemoglobins. In: Journal of Biological Chemistry. 1987 ; Vol. 262, No. 7. pp. 3044-3051.
@article{c8ed36e59953464889927fe9553158ed,
title = "Interspecies variations in the transient heme species generated subsequent to CO photolysis from hemoglobins",
abstract = "The structure, ligand binding kinetics, and thermodynamics of hemoglobin have been the subject of a great deal of investigation. However, the exact pathway(s) by which cooperative energetics are communicated within the protein remain undefined. The effects of interspecies variations in quaternary and tertiary structure, oxygen affinity, cooperativity, and ligand binding kinetics upon the overall ligand binding process are, therefore, of great importance in understanding and solving these problems. The demonstrated sensitivity of resonance Raman spectroscopy to heme structure and environment make it an ideal probe of ligand binding dynamics. It is possible to examine how specific vibrational modes change with time and correlate this with solution conditions and protein structural and conformational differences. Those modes which exhibit the greatest change with ligand photolysis are also indicative of possible paths of cooperative energy dissipation within the protein. The changes which occur in the vibrational modes of the heme within 10 ns of CO photolysis have been determined for a wide variety of mammalian and reptilian hemoglobins. The modes most affected by this process are, without exception, v(Fe-His), v4, and the substituent bending modes, δ(c(b) - s) and δ(c(b) - c(α) - c(β)). Furthermore, a direct correlation exists between the shift in porphyrin π* electron density upon CO photolysis (as indicated by the transient changes in v4) and the Hill coefficient of cooperativity. The implications of those results concerning ligand binding cooperativity in hemoglobins are discussed.",
author = "Carson, {S. D.} and Wells, {C. A.} and Findsen, {E. W.} and Friedman, {Joel M.} and Ondrias, {M. R.}",
year = "1987",
language = "English (US)",
volume = "262",
pages = "3044--3051",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "7",

}

TY - JOUR

T1 - Interspecies variations in the transient heme species generated subsequent to CO photolysis from hemoglobins

AU - Carson, S. D.

AU - Wells, C. A.

AU - Findsen, E. W.

AU - Friedman, Joel M.

AU - Ondrias, M. R.

PY - 1987

Y1 - 1987

N2 - The structure, ligand binding kinetics, and thermodynamics of hemoglobin have been the subject of a great deal of investigation. However, the exact pathway(s) by which cooperative energetics are communicated within the protein remain undefined. The effects of interspecies variations in quaternary and tertiary structure, oxygen affinity, cooperativity, and ligand binding kinetics upon the overall ligand binding process are, therefore, of great importance in understanding and solving these problems. The demonstrated sensitivity of resonance Raman spectroscopy to heme structure and environment make it an ideal probe of ligand binding dynamics. It is possible to examine how specific vibrational modes change with time and correlate this with solution conditions and protein structural and conformational differences. Those modes which exhibit the greatest change with ligand photolysis are also indicative of possible paths of cooperative energy dissipation within the protein. The changes which occur in the vibrational modes of the heme within 10 ns of CO photolysis have been determined for a wide variety of mammalian and reptilian hemoglobins. The modes most affected by this process are, without exception, v(Fe-His), v4, and the substituent bending modes, δ(c(b) - s) and δ(c(b) - c(α) - c(β)). Furthermore, a direct correlation exists between the shift in porphyrin π* electron density upon CO photolysis (as indicated by the transient changes in v4) and the Hill coefficient of cooperativity. The implications of those results concerning ligand binding cooperativity in hemoglobins are discussed.

AB - The structure, ligand binding kinetics, and thermodynamics of hemoglobin have been the subject of a great deal of investigation. However, the exact pathway(s) by which cooperative energetics are communicated within the protein remain undefined. The effects of interspecies variations in quaternary and tertiary structure, oxygen affinity, cooperativity, and ligand binding kinetics upon the overall ligand binding process are, therefore, of great importance in understanding and solving these problems. The demonstrated sensitivity of resonance Raman spectroscopy to heme structure and environment make it an ideal probe of ligand binding dynamics. It is possible to examine how specific vibrational modes change with time and correlate this with solution conditions and protein structural and conformational differences. Those modes which exhibit the greatest change with ligand photolysis are also indicative of possible paths of cooperative energy dissipation within the protein. The changes which occur in the vibrational modes of the heme within 10 ns of CO photolysis have been determined for a wide variety of mammalian and reptilian hemoglobins. The modes most affected by this process are, without exception, v(Fe-His), v4, and the substituent bending modes, δ(c(b) - s) and δ(c(b) - c(α) - c(β)). Furthermore, a direct correlation exists between the shift in porphyrin π* electron density upon CO photolysis (as indicated by the transient changes in v4) and the Hill coefficient of cooperativity. The implications of those results concerning ligand binding cooperativity in hemoglobins are discussed.

UR - http://www.scopus.com/inward/record.url?scp=0023224548&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023224548&partnerID=8YFLogxK

M3 - Article

VL - 262

SP - 3044

EP - 3051

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 7

ER -