Results 21 to 30 of about 9,358 (215)

Formate Dehydrogenase from Pseudomonas oxalaticus [PDF]

open access: yesEuropean Journal of Biochemistry, 1978
Formate dehydrogenase (EC 1.2.1.2) from Pseudomonas oxalaticus has been isolated and characterized. The enzyme (molecular weight 315000) is a complex flavoprotein containing 2 FMN, 18--25 non-heme iron atoms and 15--20 acid-labile sulphides. In the last step of the purification, a sucrose gradient centrifugation, a second catalytically active species ...
T, Höpner   +3 more
openaire   +3 more sources

A proteomic view at the biochemistry of syntrophic butyrate oxidation in Syntrophomonas wolfei. [PDF]

open access: yesPLoS ONE, 2013
In syntrophic conversion of butyrate to methane and CO2, butyrate is oxidized to acetate by secondary fermenting bacteria such as Syntrophomonas wolfei in close cooperation with methanogenic partner organisms, e.g., Methanospirillum hungatei.
Alexander Schmidt   +3 more
doaj   +1 more source

Enoyl-Coenzyme A Respiration via Formate Cycling in Syntrophic Bacteria

open access: yesmBio, 2022
Syntrophic bacteria play a key role in the anaerobic conversion of biological matter to methane. They convert short-chain fatty acids or alcohols to H2, formate, and acetate that serve as substrates for methanogenic archaea.
Michael Agne   +3 more
doaj   +1 more source

Proteomic Analysis of a Syntrophic Coculture of Syntrophobacter fumaroxidans MPOBT and Geobacter sulfurreducens PCAT

open access: yesFrontiers in Microbiology, 2021
We established a syntrophic coculture of Syntrophobacter fumaroxidans MPOBT (SF) and Geobacter sulfurreducens PCAT (GS) growing on propionate and Fe(III). Neither of the bacteria was capable of growth on propionate and Fe(III) in pure culture. Propionate
Monir Mollaei   +8 more
doaj   +1 more source

Formate dehydrogenase [PDF]

open access: yesFEMS Microbiology Letters, 1990
Formate is a substrate, or product, of diverse reactions catalyzed by eukaryotic organisms, eubacteria, and archaebacteria. A survey of metabolic groups reveals that formate is a common growth substrate, especially among the anaerobic eubacteria and archaebacteria.
openaire   +2 more sources

Energy metabolism in Mycobacterium gilvum PYR-GCK: insights from transcript expression analyses following two states of induction. [PDF]

open access: yesPLoS ONE, 2014
Mycobacterium gilvum PYR-GCK, a pyrene degrading bacterium, has been the subject of functional studies aimed at elucidating mechanisms related to its outstanding pollutant bioremediation/biodegradation activities. Several studies have investigated energy
Abimbola Comfort Badejo   +7 more
doaj   +1 more source

Core and auxiliary functions of one-carbon metabolism in Pseudomonas putida exposed by a systems-level analysis of transcriptional and physiological responses

open access: yesmSystems, 2023
The soil bacterium Pseudomonas putida is a robust biomanufacturing host that assimilates a broad range of substrates while efficiently coping with adverse environmental conditions. P. putida is equipped with functions related to one-carbon (C1) compounds
Justine Turlin   +4 more
doaj   +1 more source

NAD+-dependent Formate Dehydrogenase from Plants [PDF]

open access: yesActa Naturae, 2011
NAD(+)-dependent formate dehydrogenase (FDH, EC 1.2.1.2) widely occurs in nature. FDH consists of two identical subunits and contains neither prosthetic groups nor metal ions. This type of FDH was found in different microorganisms (including pathogenic ones), such as bacteria, yeasts, fungi, and plants. As opposed to microbiological FDHs functioning in
Alekseeva, A., Savin, S., Tishkov, V.
openaire   +3 more sources

Complete genome sequence of Syntrophobacter fumaroxidans strain (MPOB(T)). [PDF]

open access: yes, 2012
Syntrophobacter fumaroxidans strain MPOB(T) is the best-studied species of the genus Syntrophobacter. The species is of interest because of its anaerobic syntrophic lifestyle, its involvement in the conversion of propionate to acetate, H2 and CO2 during ...
Crable, Bryan R   +15 more
core   +2 more sources

Clostridium acidurici Electron-Bifurcating Formate Dehydrogenase [PDF]

open access: yesApplied and Environmental Microbiology, 2013
ABSTRACT Cell extracts of uric acid-grown Clostridium acidurici catalyzed the coupled reduction of NAD + and ferredoxin with formate at a specific activity of 1.3 U/mg. The enzyme complex catalyzing the electron-bifurcating reaction was purified 130-fold and found to be composed of ...
Wang, S.   +3 more
openaire   +3 more sources

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