Dynamics of carbon monoxide binding by heme proteins.
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.
D002248:Carbon Monoxide; D003577:Cytochrome P-450 Enzyme System / Q000302:isolation & purification; D007700:Kinetics; D008027:Light; D009211:Myoglobin; D011485:Protein Binding; D011549:Pseudomonas / Q000032:analysis; D013696:Temperature
D009211:Myoglobin; D002248:Carbon Monoxide; D003577:Cytochrome P-450 Enzyme System