Ontology highlight
ABSTRACT:
SUBMITTER: Angelastro A
PROVIDER: S-EPMC7007191 | biostudies-literature | 2019 Nov
REPOSITORIES: biostudies-literature
Angelastro Antonio A Ruiz-Pernía J Javier JJ Tuñón Iñaki I Moliner Vicent V Luk Louis Y P LYP Allemann Rudolf K RK
ACS catalysis 20190923 11
Hydride transfer is widespread in nature and has an essential role in applied research. However, the mechanisms of how this transformation occurs in living organisms remain a matter of vigorous debate. Here, we examined dihydrofolate reductase (DHFR), an enzyme that catalyzes hydride from C4' of NADPH to C6 of 7,8-dihydrofolate (H<sub>2</sub>F). Despite many investigations of the mechanism of this reaction, the contribution of polarization of the π-bond of H<sub>2</sub>F in driving hydride trans ...[more]