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 language | English (US) |
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Pages (from-to) | 1199-1205 |
Number of pages | 7 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 52 |
Issue number | 4 |
DOIs | |
State | Published - Jun 19 1973 |
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology