Using Computational Chemistry to Reveal Nature's Blueprints for Single-Site Catalysis of C–H Activation

A Nandy, H Adamji, DW Kastner, V Vennelakanti… - ACS …, 2022 - ACS Publications
The challenge of activating inert C–H bonds motivates a study of catalysts that draws from
what can be accomplished by natural enzymes and translates these advantageous features …

Influence of the greater protein environment on the electrostatic potential in metalloenzyme active sites: The case of formate dehydrogenase

A Nazemi, AH Steeves, DW Kastner… - The Journal of Physical …, 2022 - ACS Publications
The Mo/W-containing metalloenzyme formate dehydrogenase (FDH) is an efficient and
selective natural catalyst that reversibly converts CO2 to formate under ambient conditions …

Protein3D: Enabling analysis and extraction of metal‐containing sites from the Protein Data Bank with molSimplify

F Edholm, A Nandy, CR Reinhardt… - Journal of …, 2024 - Wiley Online Library
Metalloenzymes catalyze a wide range of chemical transformations, with the active site
residues playing a key role in modulating chemical reactivity and selectivity. Unlike smaller …

[HTML][HTML] Comparative analysis of CO2 reduction by soluble Escherichia coli formate dehydrogenase H and its selenocysteine-to-cysteine substitution variant

F Li, S Scheller, M Lienemann - Journal of CO2 Utilization, 2023 - Elsevier
Metal-dependent formate dehydrogenases (Me-FDHs) are highly active CO 2-reducing
enzymes operating at low redox potentials and employ either molybdenum or tungsten to …

Reactivity of a Dithiocarbamate-Ligated [WVI≡S] Complex with Hydride Donors: Toward a Synthetic Mimic of Formate Dehydrogenase

D Basu, SMS Subasinghe, NP Mankad - Inorganic chemistry, 2023 - ACS Publications
Formate dehydrogenase (FDH) enzymes catalyze redox interconversion of CO2 and HCO2–
, with a key mechanistic step being the transfer of H–from HCO2–to an oxidized active site …

CLIPZyme: Reaction-Conditioned Virtual Screening of Enzymes

PG Mikhael, I Chinn, R Barzilay - arXiv preprint arXiv:2402.06748, 2024 - arxiv.org
Computational screening of naturally occurring proteins has the potential to identify efficient
catalysts among the hundreds of millions of sequences that remain uncharacterized. Current …

Structural and biochemical characterization of the M405S variant of Desulfovibrio vulgaris formate dehydrogenase

G Vilela-Alves, R Rebelo Manuel… - … Section F: Structural …, 2024 - journals.iucr.org
Structural and biochemical characterization of the M405S variant of Desulfovibrio vulgaris
formate dehydrogenase Page 1 research communications Acta Cryst. (2024). F80 https://doi.org/10.1107/S2053230X24003911 …