Al. De Lacey et al., Simple formal kinetics for the reversible uptake of molecular hydrogen by [Ni-Fe] hydrogenase from Desulfovibrio gigas, EUR J BIOCH, 267(22), 2000, pp. 6560-6570
Enzymatic electrocatalysis, triggered and monitored by means of cyclic volt
ammetry, enabled us to achieve quantitative analysis of the kinetics of the
hydrogenase catalyzed process, in the 7.8-10.0 pH range, in the presence o
f an electrochemically generated redox mediator. The quantitative analysis
can be carried out by use of a quite simple SRC model. The simplicity of th
e SRC model is compatible with the existence of multiple redox microstates,
which can be combined in a potential adjustable triangular mechanism consi
sting of three catalytic cycles, which are formally identical from the kine
tic point of view. The steps involved in the kinetic control of the reversi
ble process are H-2 uptake or production at the Ni-Fe catalytic site and th
e intermolecular electron transfer between the mediator and the distal [4Fe
-4S] cluster. The related rate constants have been determined. For the two
accompanying intramolecular electron transfers which proceed at equilibrium
, the equilibrium constants were found to be in very good agreement with pr
eviously published data.