Resonance Raman and Site-Directed Mutagenesis Studies of Myoglobin Dynamics

  • Paul M. Champion
Part of the NATO ASI Series book series (NSSA, volume 183)


The protein structure-function relationships involved in the binding of ligands to heme proteins have been the focus of a wide variety of physical, biological and chemical investigations during the last several decades. A well studied process from an experimental point of view is the geminate recombination of CO to myoglobin:
$$Mb \cdot CO\begin{array}{*{20}{c}} \gamma \\ \rightleftarrows \\ {\left\{ k \right\}} \end{array}Mb + CO$$
Equation 1 denotes the photolysis of carbon monoxy myoglobin (MB · CO) by light (y) and the subsequent rebinding ({k}). The curly brackets around the (k) indicate that a single rate is not sufficient to describe the rebinding and that a distribution in rates is necessary to explain the non-exponential kinetics observed at low temperature (Austin et al., 1975). We believe that the distribution in rates is due to protein structural fluctuations that are frozen in below Tf (Srajer et al., 1988). Above Tf the protein fluctuations are rapid compared to kinetic time scales and a single exponential rate, averaged over the fluctuations, is observed.


Heme Protein Geminate Recombination Distal Histidine Proximal Term Distal Pocket 
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Copyright information

© Plenum Press, New York 1989

Authors and Affiliations

  • Paul M. Champion
    • 1
  1. 1.Department of PhysicsNortheastern UniversityBostonUSA

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