Toward the Mechanistic Understanding of EnzymaticCO2 Reduction
2020
Reducing CO2 is a challenging chemical transformation
that biology solves easily, with high efficiency and specificity.
In particular, formate dehydrogenases are of great interest since
they reduce CO2 to formate, a valuable chemical fuel and
hydrogen storage compound. The metal-dependent formate dehydrogenases
of prokaryotes can show high activity for CO2 reduction.
Here, we report an expression system to produce recombinant W/Sec-FdhAB
from Desulfovibrio vulgaris Hildenborough fully loaded
with cofactors, its catalytic characterization and crystal structures
in oxidized and reduced states. The enzyme has very high activity
for CO2 reduction and displays remarkable oxygen stability.
The crystal structure of the formate-reduced enzyme shows Sec still
coordinating the tungsten, supporting a mechanism of stable metal
coordination during catalysis. Comparison of the oxidized and reduced
structures shows significant changes close to the active site. The
DvFdhAB is an excellent model for studying catalytic CO2 reduction and probing the mechanism of this conversion.
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