Browsing by Author "Danson, Michael J."

Now showing items 6-10 of 17

  • Did primitive microorganisms use nonhem iron proteins in place of NAD/P?

    Daniel, Roy M.; Danson, Michael J. (Springer, 1995)
    Nicotinamide adenine dinucleotide (NAD) and nicotinamide adenine dinucleotide phosphate (NADP) are of universal occurrence in living organisms and play a central role in coupling oxidative with reductive reactions. However, ...
  • The equilibrium model for the effect of temperature on enzymes: Insights and implications

    Weinberg, Cristina S.; Daniel, Roy M.; Monk, Colin R.; Danson, Michael J.; Lee, Charles Kai-Wu (Teknoscienze SRL, 2008)
    A new, experimentally-validated “Equilibrium Model” describes the effect of temperature on enzymes, and provides a new mechanism for the reversible loss of enzyme activity with temperature. It incorporates two new, fundamental ...
  • Eurythermalism and the temperature dependence of enzyme activity

    Lee, Charles Kai-Wu; Daniel, Roy M.; Shepherd, Charis; Saul, David; Cary, S. Craig; Danson, Michael J.; Eisenthal, Robert; Peterson, Michelle E. (Federation of American Societies for Experimental Biology, 2007)
    The "Equilibrium Model" has provided new tools for describing and investigating enzyme thermal adaptation. It has been shown that the effect of temperature on enzyme activity is not only governed by ΔG‡cat and ΔG‡inact but ...
  • The molecular basis of the effect of temperature on enzyme activity

    Daniel, Roy M.; Peterson, Michelle E.; Danson, Michael J.; Price, Nicholas C.; Kelly, Sharon M.; Monk, Colin R.; Weinberg, Cristina S.; Oudshoorn, Matthew Leslie; Lee, Charles Kai-Wu (Portland Press Ltd, 2010)
    Experimental data show that the effect of temperature on enzymes cannot be adequately explained in terms of a two-state model based on increases in activity and denaturation. The Equilibrium Model provides a quantitative ...
  • A new intrinsic thermal parameter for enzymes reveals true temperature optima

    Peterson, Michelle E.; Eisenthal, Robert; Danson, Michael J.; Spence, Alastair; Daniel, Roy M. (The American Society for Biochemistry and Molecular Biology, Inc., 2004)
    Two established thermal properties of enzymes are the Arrhenius activation energy and thermal stability. Arising from anomalies found in the variation of enzyme activity with temperature, a comparison has been made of ...