US EPA

4837057 

Journal Article 

Theoretical exploration of the mechanism of formylmethanofuran dehydrogenase: the first reductive step in CO2 fixation by methanogens 

Rana, A; Dey, A 

2016 

Yes 

Journal of Biological Inorganic Chemistry
ISSN: 0949-8257
EISSN: 1432-1327 

Springer Verlag 

21 

5-6 

703-713 

English 

27456610 

10.1007/s00775-016-1377-4 

WOS:000382127000011 

A theoretical exploration of the possible active site models of methanofuran dehydrogenase reveals that the free energy of the reduction of the carbamate group is substantially negative and is driven by the electron withdrawing amide group next to the carbonyl carbon. Comparison of the computed transition state energies with the experimental energy barrier indicates that the active site is likely to have an axial oxo and equatorial hydrosulfide ligand, the substrate is likely to be protonated and a second-sphere hydrogen-bonding interaction with the axial ligand can, substantially, lower the barrier of this reaction which involves reduction of the carbonyl center of the a carbamate to form an N-formyl group via a hydride shift from a Mo(IV) center. 

Chemistry; CO2 Reduction; Computational; DFT; Mechanism; MFR-dehydrogenase; carbamic acid; carbon dioxide; formylmethanofuran dehydrogenase; oxidoreductase; unclassified drug; aldehyde dehydrogenase; formylmethanofuran dehydrogenase; Article; carbon dioxide fixation; crystal structure; energy; enzyme active site; enzyme mechanism; enzyme structure; enzyme substrate; hydrogen bond; ligand binding; mathematical model; priority journal; proton transport; chemistry; metabolism; molecular model; oxidation reduction reaction; quantum theory; thermodynamics; Aldehyde Oxidoreductases; Carbon Dioxide; Hydrogen Bonding; Models, Molecular; Oxidation-Reduction; Quantum Theory; Thermodynamics