Dynamics of Carbon Monoxide Binding by Heme Proteins
Robert H. Austin(University of Illinois Urbana-Champaign), K. W. Beeson(University of Illinois Urbana-Champaign), L. Eisenstein(University of Illinois Urbana-Champaign), Hans Frauenfelder(University of Illinois Urbana-Champaign), I. C. Gunsalus(University of Illinois Urbana-Champaign), V. P. MARSHALL(University of Illinois Urbana-Champaign)
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Abstract
Rebinding of carbon monoxide to myoglobin and to cytochrome P-450 after removal by a light flash occurs down to 50 degrees K for myoglobin and 25 degrees K for cytochrome P-450 in glycerol-water solution. Above 240 degrees K the reaction is second order; between 240 degrees and 200 degrees K the rebinding becomes exponential and independent of the carbon monoxide concentration. Below 150 degrees K the reaction follows a power law and is approximately 10(3) times faster for cytochrome P-450 than for myoglobin.
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