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Science 10 August 1973:
Vol. 181. no. 4099, pp. 541 - 543
DOI: 10.1126/science.181.4099.541
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Articles

Dynamics of Carbon Monoxide Binding by Heme Proteins

R. H. Austin 1, K. Beeson 1, L. Eisenstein 1, H. Frauenfelder 1, I. C. Gunsalus 1, and V. P. Marshall 1

1 Department of Physics and Department of Biochemistry, University of Illinois, Urbana 61801

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.


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