Dynamics of carbon monoxide binding by heme proteins

Science. 1973 Aug 10;181(4099):541-3. doi: 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 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.

MeSH terms

  • Carbon Monoxide*
  • Cytochrome P-450 Enzyme System* / isolation & purification
  • Kinetics
  • Light
  • Myoglobin*
  • Protein Binding
  • Pseudomonas / analysis
  • Temperature

Substances

  • Myoglobin
  • Carbon Monoxide
  • Cytochrome P-450 Enzyme System