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Metal-Containing Formate Dehydrogenases, a Personal View [PDF]

open access: yesMolecules, 2023
Mo/W-containing formate dehydrogenases (FDH) catalyzes the reversible oxidation of formate to carbon dioxide at their molybdenum or tungsten active sites.
Silke Leimkühler
doaj   +4 more sources

The Mechanism of Metal-Containing Formate Dehydrogenases Revisited: The Formation of Bicarbonate as Product Intermediate Provides Evidence for an Oxygen Atom Transfer Mechanism [PDF]

open access: yesMolecules, 2023
Mo/W-containing formate dehydrogenases (FDH) catalyzed the reversible oxidation of formate to carbon dioxide at their molybdenum or tungsten active sites.
Hemant Kumar   +4 more
doaj   +2 more sources

Structure and function relationship of formate dehydrogenases: an overview of recent progress [PDF]

open access: yesIUCrJ, 2023
Formate dehydrogenases (FDHs) catalyze the two-electron oxidation of formate to carbon dioxide. FDHs can be divided into several groups depending on their subunit composition and active-site metal ions.
Ami Kobayashi   +5 more
doaj   +2 more sources

Selective selC-independent selenocysteine incorporation into formate dehydrogenases. [PDF]

open access: yesPLoS ONE, 2013
The formate dehydrogenases (Fdh) Fdh-O, Fdh-N, and Fdh-H, are the only proteins in Escherichia coli that incorporate selenocysteine at a specific position by decoding a UGA codon.
Michael Zorn   +4 more
doaj   +2 more sources

Same but different: Comparison of two system-specific molecular chaperones for the maturation of formate dehydrogenases. [PDF]

open access: yesPLoS ONE, 2018
The maturation of bacterial molybdoenzymes is a complex process leading to the insertion of the bulky bis-molybdopterin guanine dinucleotide (bis-MGD) cofactor into the apo-enzyme.
Nadine Schwanhold   +3 more
doaj   +2 more sources

Mechanism of Action of Formate Dehydrogenases. [PDF]

open access: yesJ Am Chem Soc
The molybdenum- and tungsten-containing formate dehydrogenases from a variety of microorganisms catalyze the reversible interconversion of formate and CO2; several, in fact, function as CO2 reductases in the reverse direction under physiological conditions.
Niks D   +4 more
europepmc   +5 more sources

Functional expression of a Mo-dependent formate dehydrogenase in Escherichia coli under aerobic conditions. [PDF]

open access: yesPLoS ONE
BackgroundOxygen tolerant complex metal-dependent formate dehydrogenases hold potential for biotechnological applications.Principal findingsIn this work, we report the functional expression of the complex, molybdenum-dependent soluble formate ...
Marion Schulz   +8 more
doaj   +2 more sources

Highly stable and reusable immobilized formate dehydrogenases: Promising biocatalysts for in situ regeneration of NADH [PDF]

open access: yesBeilstein Journal of Organic Chemistry, 2016
This study aimed to prepare robust immobilized formate dehydrogenase (FDH) preparations which can be used as effective biocatalysts along with functional oxidoreductases, in which in situ regeneration of NADH is required.
Barış Binay   +4 more
doaj   +2 more sources

XoxF and the Calvin-Benson cycle mediate lanthanide-dependent growth on methanol in Bradyrhizobium and Sinorhizobium [PDF]

open access: yesApplied and Environmental Microbiology
Nodule-forming bacteria play crucial roles in plant health and nutrition by providing fixed nitrogen to leguminous plants. Despite the importance of this relationship, how nodule-forming bacteria are affected by plant exudates and soil minerals is not ...
Charlotte R. Mineo   +2 more
doaj   +2 more sources

How FocA facilitates fermentation and respiration of formate by Escherichia coli [PDF]

open access: yesJournal of Bacteriology
Formic acid is an important source of reductant and energy for many microorganisms. Formate is also produced as a fermentation product, e.g., by enterobacteria like Escherichia coli.
R. Gary Sawers
doaj   +2 more sources

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