Results 11 to 20 of about 6,425 (174)

A bacterial tungsten-containing aldehyde oxidoreductase forms an enzymatic decorated protein nanowire [PDF]

open access: yesScience Advances, 2023
Abstract Aldehyde oxidoreductases (AOR) are tungsten enzymes catalysing the oxidation of many different aldehydes to the corresponding carboxylic acids. In contrast to other known AORs, the enzyme from the denitrifying betaproteobacterium Aromatoleum aromaticum (AOR
Agnieszka Winiarska   +8 more
openaire   +7 more sources

Identification of crucial amino acids in mouse aldehyde oxidase 3 that determine substrate specificity. [PDF]

open access: yesPLoS ONE, 2013
In order to elucidate factors that determine substrate specificity and activity of mammalian molybdo-flavoproteins we performed site directed mutagenesis of mouse aldehyde oxidase 3 (mAOX3).
Martin Mahro   +6 more
doaj   +3 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

Purification and characterization of a benzylviologen-linked, tungsten-containing aldehyde oxidoreductase from Desulfovibrio gigas [PDF]

open access: yesJournal of Bacteriology, 1995
Desulfovibrio gigas NCIMB 9332 cells grown in ethanol-containing medium with 0.1 microM tungstate contained a benzylviologen-linked aldehyde oxidoreductase. The enzyme was purified to electrophoretic homogeneity and found to be a homodimer with a subunit M(r) of 62,000. It contained 0.68 +/- 0.08 W, 4.8 Fe, and 3.2 +/- 0.2 labile S per subunit.
HENSGENS, CMH, HAGEN, WR, HANSEN, TA
core   +7 more sources

Nicotinoprotein [NAD(P)‐containing] alcohol/aldehyde oxidoreductases [PDF]

open access: yesEuropean Journal of Biochemistry, 1993
Extracts of Gram‐positive bacteria like Rhodococcus rhodochrous, Rhodococcus erythropolis and Amycolatopsis methanolica, but not those of several Gram‐negative ones, showed dehydrogenase activity for ethanol as well as for methanol when 4‐nitroso‐N, N‐dimethylaniline (NDMA) was used as electron acceptor.
P W, Van Ophem   +2 more
openaire   +4 more sources

Coupled immobilized bi-enzymatic flow reactor employing cofactor regeneration of NAD+ using a thermophilic aldehyde dehydrogenase and lactate dehydrogenase [PDF]

open access: yes, 2023
he use of enzymes in biochemical processes is of interest due to their ability to work under mild conditions while attaining high reaction rates. A limitation in the use of enzymes such as oxidoreductases on a large scale lies with their requirement for ...
Xinxin Xiao (4849261)   +7 more
core   +4 more sources

Electrocatalytic Aldehyde Oxidation by a Tungsten Dependent Aldehyde Oxidoreductase from Aromatoleum Aromaticum

open access: yesChemistry – A European Journal, 2023
AbstractIn contrast to their molybdenum dependent relatives, tungsten enzymes operate at significantly lower redox potentials, and in some cases they can carry out reversible redox transformations of their substrates and products. Still, the electrochemical properties of W enzymes have received much less attention than their Mo relatives.
Palraj Kalimuthu   +6 more
openaire   +4 more sources

Electron Microscopic Analysis and Structural Characterization of Novel NADP(H)-Containing Methanol: N,N'-Dimethyl-4-Nitrosoaniline Oxidoreductases from the Gram-Positive Methylotrophic Bacteria Amycolatopsis methanolica and Mycobacterium gastri MB19 [PDF]

open access: yes, 1993
The quaternary protein structure of two methanol:N,N'-dimethyl-4-nitrosoaniline (NDMA) oxidoreductases purified from Amycolatopsis methanolica and Mycobacterium gastri MB19 was analyzed by electron microscopy and image processing.
Bruggen, Ernst F.J. van,   +23 more
core   +6 more sources

Direct electrochemistry of the Desulfovibrio gigas aldehyde oxidoreductase [PDF]

open access: yesEuropean Journal of Biochemistry, 2004
This work reports on the direct electrochemistry of the Desulfovibrio gigas aldehyde oxidoreductase (DgAOR), a molybdenum enzyme of the xanthine oxidase family that contains three redox‐active cofactors: two [2Fe‐2S] centers and a molybdopterin cytosine dinucleotide cofactor.
Margarida M, Correia dos Santos   +5 more
openaire   +2 more sources

Membrane electrochemical reactors (MER) for NADH regeneration in HLADH-catalysed synthesis: comparison of effectiveness [PDF]

open access: yes, 2004
Two membrane electrochemical reactors(MER) were designed and applied to HLADH-catalysed reduction of cyclohexanone to cyclohexanol. The regeneration of the cofactor NADH was ensured electrochemically, using either methyl viologen or a rhodium complex as
Basséguy, Régine   +2 more
core   +1 more source

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