Martín R, Díez V, Burgos J
Biochim Biophys Acta. 1976 Apr 8;429(2):293-300. doi: 10.1016/0005-2744(76)90277-1.
(1) The pH dependence of the kinetic parameters of the reaction catalyzed by pigeon liver diacetyl reductase (EC 1.1.1.5) was investigated in the pH range 5.1-8.6. (2) From the results obtained it is postulated that: (a), a group of pK around 7, active in the protonated form, participates in the interaction of the enzyme with NADH and NAD. (b), a second group with a pK of 8.4, active in the protonated form too, takes part in the binding of diacetyl to E-NADH. (c) A third group of pK about 4.7-5, active in the unprotonated form, is involved at least in the dissociation of the complex E-NAD and in the attachment of diacetyl to E-NADH.