Kinetic analysis of dye-linked dehydrogenases and related enzymes where the electron acceptor binds twice during the catalytic sequence

This publication has 16 references indexed in Scilit:

• Phenazine ethosulfate as a preferred electron acceptor to phenazine methosulfate in dye-linked enzyme assays
  Analytical Biochemistry, 1979
• Steady-state investigations of the mechanism of histidinol dehydrogenase
  Biochemical Journal, 1979
• The quantitative analysis of ligand binding and initial-rate data for allosteric and other complex enzyme mechanisms
  Biochemical Journal, 1976
• Sigmoid curves, non-linear double-reciprocal plots and allosterism
  Biochemical Journal, 1975
• The mechanistic interpretation of initial velocity and product inhibition data arising from enzyme catalysed reactions whose catalytic cycle is unbranched
  Journal of Theoretical Biology, 1975
• The acceptor specificity of flavins and flavoproteins. III. Flavoproteins
  Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1971
• A comparative study of some mechanisms describing interaction effects in a dimeric, two-substrate enzyme catalysed reaction
  Journal of Theoretical Biology, 1968
• The interpretation of non-hyperbolic rate curves for two-substrate enzymes. A possible mechanism for phosphofructokinase
  Biochemical Journal, 1966
• The kinetics of enzyme-catalyzed reactions with two or more substrates or products
  Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 1963
• Typical behaviour of some simple models of enzyme action
  Transactions of the Faraday Society, 1958