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Updated: Apr 17, 2026

Author Spotlight: Magnetometric Characterization of Intermediates in the Solid-State Electrochemistry of Redox-Active Metal-Organic Frameworks
Published on: June 9, 2023
Theoretical studies on mechanisms of some Mo enzymes
Nuno M F S A Cerqueira1, Bholanath Pakhira, Sabyasachi Sarkar
1REQUIMTE, Departamento de Química, Faculdade de Ciências, Universidade do Porto, Rua do Campo Alegre s/n, 4169-007, Porto, Portugal, nscerque@fc.up.pt.
Abstract:
Modeling of molybdoenzymes began even before the knowledge of the three-dimensional structure of these enzymes. The theoretical and experimental knowledge on these enzymes is vast and newer investigation is regularly pursued to understand the electronic aspect of these proteins using computational means. The present review deals with some unique observation regarding the structure, function and reactivity of some models and native proteins in rationalizing the choice of diverse substrates in seemingly similar enzymes such as Nap (nitrate reductase) and Fdh (formate dehydrogenase) and the dual form of a specific substrate of an enzyme like trimethylamine N-oxide reductase (TAMOR) and providing the electronic reason for the inhibition in the oxypurinol-inhibited xanthine oxidase (XO).
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