Kinetic origin of the pronounced bohr effect in an annelid hemoglobin

K. J. Wiechelman, L. J. Parkhurst

Research output: Contribution to journalArticlepeer-review

9 Scopus citations

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

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint

Dive into the research topics of 'Kinetic origin of the pronounced bohr effect in an annelid hemoglobin'. Together they form a unique fingerprint.

Cite this