Understanding the mechanisms and kinetics of enzymatic reactions is essential for studies
of life science and for bioengineering. Here the different reaction states in the catalytic cycle …

The structure of formate dehydrogenase from Candida boidinii (CbFDH) is of both academic
and practical interests. First, this enzyme represents a unique model system for studies on …

Formate dehydrogenase from Candida boidinii (CboFDH) catalyses the oxidation of formate
anion to carbon dioxide with concomitant reduction of NAD+ to NADH. CboFDH is highly …

Thermal motions of enzymes have been invoked to explain the temperature dependence of
kinetic isotope effects (KIEs) in enzyme-catalyzed hydride transfers. Formate …

Protein dynamics have controversially been proposed to be at the heart of enzyme catalysis,
but identification and analysis of dynamical effects in enzyme-catalyzed reactions have …

Multistep enzyme-catalyzed cascade reactions are highly efficient in nature due to the
confinement and concentration of the enzymes within nanocompartments. In this way, rates …

Formate dehydrogenase (FDH) from Pseudomonas sp. 101 is a homodimeric enzyme that
catalyzes oxidation of formate and the concomitant reduction of NAD+ to produce NADH and …

Metal-dependent formate dehydrogenases (FDHs) catalyze the reversible conversion of
formate into CO2, a proton, and two electrons. Kinetic studies of FDHs provide key insights …

The understanding of the mechanism of enzymatic recovery of NADH is of biological and of
considerable biotechnological interest, since the essential, but expensive, cofactor NADH is …

NAD+-dependent formate dehydrogenase (FDH) from Candida boidinii was cloned and
expressed to a high level in Escherichia coli (20% of soluble E. coli protein). Molecular …