Iac. Pereira et al., ELECTRON-TRANSFER BETWEEN HYDROGENASES AND MONOHEME AND MULTIHEME CYTOCHROMES IN DESULFOVIBRIO SSP, JBIC. Journal of biological inorganic chemistry, 3(5), 1998, pp. 494-498
A comparative study of electron transfer between the 16 heme high mole
cular mass cytochrome (Hmc) from Kesulfovibrio vulgaris Hildenborough
and the [Fe] and [NiFe] hydrogenases from the same organism was carrie
d out, both in the presence and in the absence of catalytic amounts of
cytochrome Cg. For comparison, this study was repeated with the [NiFe
] hydrogenase from D. gigas. Hmc is very slowly reduced by the [Fe] hy
drogenase, but faster by either of the two [NiFe] hydrogenases. In the
presence of cytochrome c(3), in equimolar amounts to the hydrogenases
, the rates of electron transfer are significantly increased and are s
imilar for the three hydrogenases. The results obtained indicate that
the reduction of Hmc by the [Fe] or [NiFe] hydrogenases is most likely
mediated by cytochrome c(3). A similar study with D. vulgaris Hildenb
orough cytochrome C-553 shows that, in contrast, this cytochrome is re
duced faster by the [Fe] hydrogenase than by the [NiFe] hydrogenases.
However, although catalytic amounts of cytochrome c3 have no effect in
the reduction by the [Fe] hydrogenase, it significantly increases the
rate of reduction by the [NiFe] hydrogenases.