Kinetic origin of the pronounced bohr effect in an annelid hemoglobin

K. J. Wiechelman, Lawrence J Parkhurst

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

The kinetics of oxygen and CO binding by the high molecular weight hemoglobin (ca. 3,000,000) from the annelid Cirraformia grandis have been measured by stopped-flow and flash-photolysis as a function of pH. Flash-photolysis studies of the Hb* form suggest weak heme-heme interaction for ligand binding in the ferrous state. The rate constant for oxygen dissociation increases by a factor of ca. 800 from pH 9 to pH 6. Rate constants for oxygen and CO association are virtually unchanged in the range pH 6-9.

Original languageEnglish (US)
Pages (from-to)1199-1205
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume52
Issue number4
DOIs
StatePublished - Jun 19 1973

Fingerprint

Hemoglobins
Photolysis
Carbon Monoxide
Oxygen
Heme
Kinetics
Rate constants
Molecular weight
Association reactions
Ligands
Molecular Weight

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Kinetic origin of the pronounced bohr effect in an annelid hemoglobin. / Wiechelman, K. J.; Parkhurst, Lawrence J.

In: Biochemical and Biophysical Research Communications, Vol. 52, No. 4, 19.06.1973, p. 1199-1205.

Research output: Contribution to journalArticle

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