Tertiary-structure relaxation in hemoglobin: A transient Raman study

T. W. Scott, Joel M. Friedman

Research output: Contribution to journalArticle

108 Citations (Scopus)

Abstract

Tertiary relaxation in photodissociated hemoglobins has been monitored by using time-resolved resonance Raman scattering. It is observed that the submicrosecond tertiary-structure relaxation which precedes the switch in quarternary structure is sensitive to factors influencing R state stability. At pH 7 and lower, substantial relaxation involving the iron-proximal histidine linkage occurs over the time scale of geminate recombination. Because the structural parameter associated with the variation in this linkage has been implicated in the protein modulation of ligand binding, this result supports the idea of a dynamic barrier which increases on the time scale of geminate recombination. On the basis of these findings a model is presented which accounts for solution-dependent variations in ligand reactivity within a given quaternary structure.

Original languageEnglish (US)
Pages (from-to)5677-5687
Number of pages11
JournalJournal of the American Chemical Society
Volume106
Issue number19
StatePublished - Jan 1 1984
Externally publishedYes

Fingerprint

Hemoglobin
Hemoglobins
Ligands
Genetic Recombination
Histidine
Raman scattering
Iron
Raman Spectrum Analysis
R Factors
Switches
Modulation
Proteins

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Tertiary-structure relaxation in hemoglobin : A transient Raman study. / Scott, T. W.; Friedman, Joel M.

In: Journal of the American Chemical Society, Vol. 106, No. 19, 01.01.1984, p. 5677-5687.

Research output: Contribution to journalArticle

@article{91494ab8d20947fab5fd6dce01826eab,
title = "Tertiary-structure relaxation in hemoglobin: A transient Raman study",
abstract = "Tertiary relaxation in photodissociated hemoglobins has been monitored by using time-resolved resonance Raman scattering. It is observed that the submicrosecond tertiary-structure relaxation which precedes the switch in quarternary structure is sensitive to factors influencing R state stability. At pH 7 and lower, substantial relaxation involving the iron-proximal histidine linkage occurs over the time scale of geminate recombination. Because the structural parameter associated with the variation in this linkage has been implicated in the protein modulation of ligand binding, this result supports the idea of a dynamic barrier which increases on the time scale of geminate recombination. On the basis of these findings a model is presented which accounts for solution-dependent variations in ligand reactivity within a given quaternary structure.",
author = "Scott, {T. W.} and Friedman, {Joel M.}",
year = "1984",
month = "1",
day = "1",
language = "English (US)",
volume = "106",
pages = "5677--5687",
journal = "Journal of the American Chemical Society",
issn = "0002-7863",
publisher = "American Chemical Society",
number = "19",

}

TY - JOUR

T1 - Tertiary-structure relaxation in hemoglobin

T2 - A transient Raman study

AU - Scott, T. W.

AU - Friedman, Joel M.

PY - 1984/1/1

Y1 - 1984/1/1

N2 - Tertiary relaxation in photodissociated hemoglobins has been monitored by using time-resolved resonance Raman scattering. It is observed that the submicrosecond tertiary-structure relaxation which precedes the switch in quarternary structure is sensitive to factors influencing R state stability. At pH 7 and lower, substantial relaxation involving the iron-proximal histidine linkage occurs over the time scale of geminate recombination. Because the structural parameter associated with the variation in this linkage has been implicated in the protein modulation of ligand binding, this result supports the idea of a dynamic barrier which increases on the time scale of geminate recombination. On the basis of these findings a model is presented which accounts for solution-dependent variations in ligand reactivity within a given quaternary structure.

AB - Tertiary relaxation in photodissociated hemoglobins has been monitored by using time-resolved resonance Raman scattering. It is observed that the submicrosecond tertiary-structure relaxation which precedes the switch in quarternary structure is sensitive to factors influencing R state stability. At pH 7 and lower, substantial relaxation involving the iron-proximal histidine linkage occurs over the time scale of geminate recombination. Because the structural parameter associated with the variation in this linkage has been implicated in the protein modulation of ligand binding, this result supports the idea of a dynamic barrier which increases on the time scale of geminate recombination. On the basis of these findings a model is presented which accounts for solution-dependent variations in ligand reactivity within a given quaternary structure.

UR - http://www.scopus.com/inward/record.url?scp=0021486088&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0021486088&partnerID=8YFLogxK

M3 - Article

AN - SCOPUS:0021486088

VL - 106

SP - 5677

EP - 5687

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

SN - 0002-7863

IS - 19

ER -