Kinetics of oxygen and carbon monoxide binding to liver fluke (Dicrocoelium dendriticum) hemoglobin. An extreme case?

E. E. Di Iorio, U. Thomas Meier, J. D G Smit, K. H. Winterhalter

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

The kinetics of oxygen and carbon monoxide binding to the monomeric liver fluke (Dicrocoelium dendriticum) hemoglobin have been studied. The ligand association rates are ~1 x 108 and ~3 x 108 M-1 s-1, respectively, for CO and O2 and show no pH dependence. On the contrary the ligand dissociation rates decrease by lowering the pH below 7, the pK of the transition being around 5.5. These findings, together with spectroscopic properties of the protein, are discussed in ralation to the fact that, in this hemoglobin, the distal histidine is replaced by a glycine.

Original languageEnglish (US)
Pages (from-to)2160-2164
Number of pages5
JournalJournal of Biological Chemistry
Volume260
Issue number4
StatePublished - Jan 1 1985
Externally publishedYes

Fingerprint

Dicrocoelium
Fasciola hepatica
Carbon Monoxide
Liver
Hemoglobins
Oxygen
Ligands
Kinetics
Histidine
Glycine
Association reactions
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

Kinetics of oxygen and carbon monoxide binding to liver fluke (Dicrocoelium dendriticum) hemoglobin. An extreme case? / Di Iorio, E. E.; Meier, U. Thomas; Smit, J. D G; Winterhalter, K. H.

In: Journal of Biological Chemistry, Vol. 260, No. 4, 01.01.1985, p. 2160-2164.

Research output: Contribution to journalArticle

@article{0f674f1a77994fa2b5a0895c8d5c7532,
title = "Kinetics of oxygen and carbon monoxide binding to liver fluke (Dicrocoelium dendriticum) hemoglobin. An extreme case?",
abstract = "The kinetics of oxygen and carbon monoxide binding to the monomeric liver fluke (Dicrocoelium dendriticum) hemoglobin have been studied. The ligand association rates are ~1 x 108 and ~3 x 108 M-1 s-1, respectively, for CO and O2 and show no pH dependence. On the contrary the ligand dissociation rates decrease by lowering the pH below 7, the pK of the transition being around 5.5. These findings, together with spectroscopic properties of the protein, are discussed in ralation to the fact that, in this hemoglobin, the distal histidine is replaced by a glycine.",
author = "{Di Iorio}, {E. E.} and Meier, {U. Thomas} and Smit, {J. D G} and Winterhalter, {K. H.}",
year = "1985",
month = "1",
day = "1",
language = "English (US)",
volume = "260",
pages = "2160--2164",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "4",

}

TY - JOUR

T1 - Kinetics of oxygen and carbon monoxide binding to liver fluke (Dicrocoelium dendriticum) hemoglobin. An extreme case?

AU - Di Iorio, E. E.

AU - Meier, U. Thomas

AU - Smit, J. D G

AU - Winterhalter, K. H.

PY - 1985/1/1

Y1 - 1985/1/1

N2 - The kinetics of oxygen and carbon monoxide binding to the monomeric liver fluke (Dicrocoelium dendriticum) hemoglobin have been studied. The ligand association rates are ~1 x 108 and ~3 x 108 M-1 s-1, respectively, for CO and O2 and show no pH dependence. On the contrary the ligand dissociation rates decrease by lowering the pH below 7, the pK of the transition being around 5.5. These findings, together with spectroscopic properties of the protein, are discussed in ralation to the fact that, in this hemoglobin, the distal histidine is replaced by a glycine.

AB - The kinetics of oxygen and carbon monoxide binding to the monomeric liver fluke (Dicrocoelium dendriticum) hemoglobin have been studied. The ligand association rates are ~1 x 108 and ~3 x 108 M-1 s-1, respectively, for CO and O2 and show no pH dependence. On the contrary the ligand dissociation rates decrease by lowering the pH below 7, the pK of the transition being around 5.5. These findings, together with spectroscopic properties of the protein, are discussed in ralation to the fact that, in this hemoglobin, the distal histidine is replaced by a glycine.

UR - http://www.scopus.com/inward/record.url?scp=0021996705&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0021996705&partnerID=8YFLogxK

M3 - Article

VL - 260

SP - 2160

EP - 2164

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 4

ER -