Results 1 to 10 of about 8,399 (179)

Characterization of human oxidoreductases involved in aldehyde odorant metabolism. [PDF]

open access: yesSci Rep, 2023
AbstractOxidoreductases are major enzymes of xenobiotic metabolism. Consequently, they are essential in the chemoprotection of the human body. Many xenobiotic metabolism enzymes have been shown to be involved in chemosensory tissue protection. Among them, some were additionally shown to be involved in chemosensory perception, acting in signal ...
Boichot V   +12 more
europepmc   +9 more sources

Biosynthetic Strategies of Berberine Bridge Enzyme-like Flavoprotein Oxidases toward Structural Diversification in Natural Product Biosynthesis. [PDF]

open access: yesBiochemistry
Berberine bridge enzyme-like oxidases are often involved in natural product biosynthesis and are seen as essential enzymes for the generation of intricate pharmacophores.
Tjallinks G, Mattevi A, Fraaije MW.
europepmc   +3 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.
José J. G. Moura   +5 more
openaire   +3 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   +2 more sources

Supersulfide biology and translational medicine for disease control

open access: yesBritish Journal of Pharmacology, EarlyView., 2023
Abstract For decades, the major focus of redox biology has been oxygen, the most abundant element on Earth. Molecular oxygen functions as the final electron acceptor in the mitochondrial respiratory chain, contributing to energy production in aerobic organisms. In addition, oxygen‐derived reactive oxygen species including hydrogen peroxide and nitrogen
Uladzimir Barayeu   +5 more
wiley   +1 more source

Tungsten‐containing aldehyde oxidoreductase of Eubacterium acidaminophilum [PDF]

open access: yesEuropean Journal of Biochemistry, 2003
Aldehyde oxidoreductase of Eubacterium acidaminophilum was purified to homogeneity under strict anaerobic conditions using a four‐step procedure. The purified enzyme was present as a monomer with an apparent molecular mass of 67 kDa and contained 6.0 ± 0.1 iron, 1.1 ± 0.2 tungsten, about 0.6 mol pterin cofactor and zinc, but no molybdenum.
Jan R. Andreesen   +4 more
openaire   +3 more sources

The oxygen-independent metabolism of cyclic monoterpenes in Castellaniella defragrans 65Phen [PDF]

open access: yes, 2014
BACKGROUND: The facultatively anaerobic betaproteobacterium Castellaniella defragrans 65Phen utilizes acyclic, monocyclic and bicyclic monoterpenes as sole carbon source under oxic as well as anoxic conditions.
Becher, D.   +7 more
core   +2 more sources

Comparative genomics and mutagenesis analyses of choline metabolism in the marine Roseobacter clade [PDF]

open access: yes, 2015
Choline is ubiquitous in marine eukaryotes and appears to be widely distributed in surface marine waters; however, its metabolism by marine bacteria is poorly understood.
Andresen P.A.   +6 more
core   +1 more source

Immunochemical characterization of aldo-keto reductases from human tissues [PDF]

open access: yes, 1985
Aldose reductase, aldehyde reductase and carbonyl reductase constitute a family of monomeric NADPH-dependent oxidoreductases with similar physical and chemical properties.
Wermuth, Bendicht, Wirth, Hans-Peter
core   +1 more source

Multiple implications of an active site phenylalanine in the catalysis of aryl-alcohol oxidase [PDF]

open access: yes, 2018
Aryl-alcohol oxidase (AAO) has demonstrated to be an enzyme with a bright future ahead due to its biotechnological potential in deracemisation of chiral compounds, production of bioplastic precursors and other reactions of interest.
Amengual-Rigo, Pep   +6 more
core   +6 more sources

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