Dimethylsulfoxide (DMSO) reductase a member of the DMSO reductase family of molybdenum enzymes
, 2009 Herein we describe the application of continuous wave (CW) and pulsed EPR spectroscopy to the structural (geometric and electronic) characterization of the Mo(V) active site within dimethylsulfoxide (DMSO)reductase and where appropriate, model molybdenum(
Ian Lane +2 more
core +5 more sources
Methane, arsenic, selenium and the origins of the DMSO reductase family. [PDF]
Sci Rep, 2020 AbstractMononuclear molybdoenzymes of the dimethyl sulfoxide reductase (DMSOR) family catalyze a number of reactions essential to the carbon, nitrogen, sulfur, arsenic, and selenium biogeochemical cycles. These enzymes are also ancient, with many lineages likely predating the divergence of the last universal common ancestor into ...
Wells M +6 more
europepmc +4 more sources
The use of dimethylsulfoxide as a solvent in enzyme inhibition studies: the case of aldose reductase [PDF]
Journal of Enzyme Inhibition and Medicinal Chemistry, 2017 Aldose reductase (AR) is an enzyme devoted to cell detoxification and at the same time is strongly involved in the aetiology of secondary diabetic complications and the amplification of inflammatory phenomena.
Livia Misuri +6 more
doaj +2 more sources
Detection of the optical bands of molybdenum(V) in DMSO reductase (Rhodobacter capsulatus) by low-temperature MCD spectroscopy [PDF]
FEBS Letters, 1992 Dimethylsulphoxide (DMSO) reductase from R. capsulatus contains a molybdenum-pterin cofactor at its active site. As prepared the molybdenum is in the 6+ oxidation state, devoid of EPR signals.
Farrar, Jaqui A. +7 more
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Reduction of Protein Bound Methionine Sulfoxide by a Periplasmic Dimethyl Sulfoxide Reductase
Antioxidants, 2020 In proteins, methionine (Met) can be oxidized into Met sulfoxide (MetO). The ubiquitous methionine sulfoxide reductases (Msr) A and B are thiol-oxidoreductases reducing MetO.
Lionel Tarrago +9 more
doaj +1 more source
Assembly pathway of a bacterial complex iron sulfur molybdoenzyme
Biomolecular Concepts, 2017 Protein folding and assembly into macromolecule complexes within the living cell are complex processes requiring intimate coordination. The biogenesis of complex iron sulfur molybdoenzymes (CISM) requires use of a system specific chaperone – a redox ...
Cherak Stephana J., Turner Raymond J.
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Spectroscopic Studies of Mononuclear Molybdenum Enzyme Centers
Molecules, 2022 A concise review is provided of the contributions that various spectroscopic methods have made to our understanding of the physical and electronic structures of mononuclear molybdenum enzymes.
Martin L. Kirk, Russ Hille
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Redox characteristics of the tungsten DMSO reductase of Rhodobacter capsulatus
FEBS Letters, 2003 The dimethylsulfoxide reductase (DMSOR) from Rhodobacter capsulatus is known to retain its three‐dimensional structure and enzymatic activity upon substitution of molybdenum, the metal that occurs naturally at the active site, by tungsten. The redox properties of tungsten‐substituted DMSOR (W‐DMSOR) have been investigated by a dye‐mediated reductive ...
Hagedoorn, Peter-Leon +5 more
openaire +2 more sources
All-trans retinoic acid has renoprotective effects on Cisplatin-induced acute kidney injury in rats. [PDF]
Alfarama Journal of Basic & Applied Sciences, 2021 All-trans retinoic acid (ATRA) is the active metabolites of vitamin A; it has antioxidant effects, and can regulate apoptosis. This study aims to observe the effects of ATRA on cisplatin-induced acute kidney injury, where a total of 96 Sprague-Dawley ...
Faten Zahran +3 more
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mBio, 2017 Methionine sulfoxide reductase A (MsrA) is an antioxidant enzyme found in all domains of life that catalyzes the reduction of methionine-S-sulfoxide (MSO) to methionine in proteins and free amino acids.
Xian Fu +7 more
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