Dynamics of Carbon Monoxide Binding by Heme Proteins
- 10 August 1973
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 181 (4099) , 541-543
- https://doi.org/10.1126/science.181.4099.541
Abstract
Rebinding of carbon monoxide to myoglobin and to cytochrome P-450 after removal by a light flash occurs down to 50°K for myoglobin and 25°K for cytochrome P-450 in glycerol-water solution. Above 240°K the reaction is second order; between 240° and 200°K the rebinding becomes exponential and independent of the carbon monoxide concentration. Below 150°K the reaction follows a power law and is approximately 103 times faster for cytochrome P-450 than for myoglobin.Keywords
This publication has 3 references indexed in Scilit:
- Carbon monoxide binding by Pseudomonas putida cytochrome P-450Archives of Biochemistry and Biophysics, 1972
- Crystalline cytochrome P-450camBiochemical and Biophysical Research Communications, 1970
- An apparatus for flash photolysis and its application to the reactions of myoglobin with gasesThe Journal of Physiology, 1956