Related Experiment Video
Updated: Jul 29, 2026

Temperature-programmed Deoxygenation of Acetic Acid on Molybdenum Carbide Catalysts
Published on: February 7, 2017
Characterization and spectroscopic properties of reduced Mo and W formate dehydrogenase from C. thermoaceticum
Abstract:
Formate dehydrogenase (FDH) (EC 1.2.1.43) from C. thermoaceticum has been purified in two forms. One contains tungsten (W), and the other is enriched in molybdenum (Mo). The W-FDH is clearly active, while the Mo results are ambiguous with enzymatic activities generally lower in the Mo-enriched samples. Spectroscopic studies (EPR, absorption, and CD) on W-FDH and Mo-FDH demonstrate that no signal correlates to the group VI metal active site in the dithionite-reduced enzyme. This lack of a W(V) EPR signal is in contrast to the results observed for tungsten-substituted sulfite oxidase which is inactive.
More Related Videos
Related Concept Videos
Role of Reduced Coenzymes NADH and FADH₂
Oxidation and Reduction of Organic Molecules
The removal of an electron from a molecule, results in a...
Redox Titration: Other Oxidizing and Reducing Agents
![Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase](/_next/image?url=https%3A%2F%2Fcloudfront.jove.com%2FCDNSource%2Fteasers%2F55858.jpg&w=3840&q=50)
