Results 41 to 50 of about 9,358 (215)

Transcriptional Response of Selenopolypeptide Genes and Selenocysteine Biosynthesis Machinery Genes in Escherichia coli during Selenite Reduction [PDF]

open access: yes, 2014
This work was supported by a United States Department of Agriculture-Cooperative State Research, Education, and Extension Service grant (no. 2009-35318-05032), a Biotechnology Research grant (no.
Tetteh, Antonia Y.   +6 more
core   +2 more sources

Protein Mass Effects on Formate Dehydrogenase [PDF]

open access: yesJournal of the American Chemical Society, 2017
Isotopically labeled enzymes (denoted as "heavy" or "Born-Oppenheimer" enzymes) have been used to test the role of protein dynamics in catalysis. The original idea was that the protein's higher mass would reduce the frequency of its normal-modes without altering its electrostatics.
Chethya Ranasinghe   +6 more
openaire   +2 more sources

Reversible interconversion of CO2 and formate by a molybdenum-containing formate dehydrogenase. [PDF]

open access: yes, 2014
CO2 and formate are rapidly, selectively, and efficiently interconverted by tungsten-containing formate dehydrogenases that surpass current synthetic catalysts.
Bassegoda, Arnau   +4 more
core   +2 more sources

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

open access: yesJournal of CO2 Utilization, 2023
Metal-dependent formate dehydrogenases (Me-FDHs) are highly active CO2-reducing enzymes operating at low redox potentials and employ either molybdenum or tungsten to reduce the bound substrate.
Feilong Li   +2 more
doaj   +1 more source

Functional responses of methanogenic archaea to syntrophic growth. [PDF]

open access: yes, 2012
Methanococcus maripaludis grown syntrophically with Desulfovibrio vulgaris was compared with M. maripaludis monocultures grown under hydrogen limitation using transcriptional, proteomic and metabolite analyses.
Arkin, Adam P   +13 more
core   +2 more sources

Structural Insights Into CO2 Transport Pathways in a W‐Formate Dehydrogenase: Structural Basis for CO2 Reduction

open access: yesAngewandte Chemie, EarlyView.
Integrated structural analysis of N. vulgaris formate dehydrogenase AB, an enzyme with applications in climate change mitigation, is reported. The substrate/product diffusion pathways were fully mapped, and a retention site was identified that transiently holds substrates and has a key role in CO2‐reducing activity.
Guilherme Vilela‐Alves   +8 more
wiley   +2 more sources

Some Properties of Formate Dehydrogenase

open access: yesZeitschrift für Naturforschung B, 1972
The enzyme was anaerobically isolated and was characterized as a flavoprotein containing at least 1 FMN, 5-8 Fe and 7-8 moles labile sulfide per mole (M. W. appr. 300.000). It catalyzes the oxidation of formate by NAD, O2 (forming H2O2) and dyes and the oxidation of NADH by O2 (forming Η2Ο2) and dyes. It is irreversibly inhibited by formate.
T, Höpner, A, Trautwein
openaire   +2 more sources

Bioelectrochemical conversion of CO2 to value added product formate using engineered Methylobacterium extorquens [PDF]

open access: yes, 2018
The conversion of carbon dioxide to formate is a fundamental step for building C1 chemical platforms. Methylobacterium extorquens AM1 was reported to show remarkable activity converting carbon dioxide into formate.
A Bassegoda   +32 more
core   +1 more source

Genetic and Phenotypic Comparison of Facultative Methylotrophy between Methylobacterium extorquens Strains PA1 and AM1 [PDF]

open access: yes, 2014
Methylobacterium extorquens AM1, a strain serendipitously isolated half a century ago, has become the best-characterized model system for the study of aerobic methylotrophy (the ability to grow on reduced single-carbon compounds).
Marx, Christopher J., Nayak, Dipti D.
core   +7 more sources

Biocatalytic cofactor regeneration for CO2 reduction: Integration of a hydrogenase and a formate dehydrogenase in H2-driven systems

open access: yesJournal of CO2 Utilization
Formate dehydrogenases catalyze the reversible oxidation of formate to carbon dioxide. These enzymes play an important role in CO2 reduction and serve as nicotinamide cofactor recycling enzymes.
Michael Groh   +5 more
doaj   +1 more source

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