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Mediated Electrochemistry of DMSO Reductase from Rhodobacter capsulatus [PDF]
, 2023 A series of macrocyclic FeIII/II and CoIII/II transition metal complexes has been selected and tested to serve as artificial mediators in redox potentiometry of proteins and also in catalytic cyclic voltammetry of redox active enzymes. The potentials of these mediators ranges approximately from +200 mV to -600 mV vs the normal hydrogen electrode (NHE ...
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The nature and function of the catalytic centres of the DMSO reductasesâ€
Dalton Transactions, 2005Density functional theory calculations have been performed to probe aspects of the function of the reaction centres of the DMSO reductase enzymes, in respect of catalysis of oxygen atom transfer (OAT). The first comparison between Mo and W at the active site of these enzymes has been accomplished by a consideration of the reaction profile for OAT from ...
Jonathan P McNamara +2 more
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Environmental Microbiology Reports, 2020
Summary The dimethylsulfoxide (DMSO) reductase family of enzymes has many subfamilies catalysing unique biogeochemical reactions. It also has many uncharacterized subfamilies. Comparative genomics predicted one such subfamily to participate in a key step of the chlorine cycle because of a conserved genetic ...
Tyler P. Barnum, John D. Coates
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Summary The dimethylsulfoxide (DMSO) reductase family of enzymes has many subfamilies catalysing unique biogeochemical reactions. It also has many uncharacterized subfamilies. Comparative genomics predicted one such subfamily to participate in a key step of the chlorine cycle because of a conserved genetic ...
Tyler P. Barnum, John D. Coates
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Electrochemical enzymatic deoxygenation of chiral sulfoxides utilizing DMSO reductase
Tetrahedron: Asymmetry, 2000Abstract Preparation of enantiomerically enriched sulfoxides by an electrochemical enzymatic system utilizing DMSO reductase was studied. This system consists of a glassy carbon electrode as the working electrode, methyl viologen as the mediator and DMSO reductase from Rhodobacter sphaeroides f. sp. denitrificans as the catalyst.
Mitsuru Abo, Sunao Yamazaki, Akira Okubo
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JBIC Journal of Biological Inorganic Chemistry, 2020
The molybdopterin enzyme family catalyzes a variety of substrates and plays a critical role in the cycling of carbon, nitrogen, arsenic, and selenium. The dimethyl sulfoxide reductase (DMSOR) subfamily is the most diverse family of molybdopterin enzymes and the members of this family catalyze a myriad of reactions that are important in microbial life ...
Breeanna Mintmier +3 more
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The molybdopterin enzyme family catalyzes a variety of substrates and plays a critical role in the cycling of carbon, nitrogen, arsenic, and selenium. The dimethyl sulfoxide reductase (DMSOR) subfamily is the most diverse family of molybdopterin enzymes and the members of this family catalyze a myriad of reactions that are important in microbial life ...
Breeanna Mintmier +3 more
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Bioorganic and Medicinal Chemistry Letters, 2020
Aldose reductase (AR) inhibitors are used clinically to treat long-term diabetic complications. Previous studies reported a series of AR inhibitory candidates, but unfortunately the mode of inhibition was poorly described due mainly to the lack of readily available methods for evaluating the specificity.
Takeru Nose +2 more
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Aldose reductase (AR) inhibitors are used clinically to treat long-term diabetic complications. Previous studies reported a series of AR inhibitory candidates, but unfortunately the mode of inhibition was poorly described due mainly to the lack of readily available methods for evaluating the specificity.
Takeru Nose +2 more
exaly +3 more sources
Resonance Raman Spectroscopic Characterization of the Molybdopterin Active Site of DMSO Reductase
Biochemistry, 1995Resonance Raman spectra are compared for Rhodobacter sphaeroides dimethyl sulfoxide reductase, an enzyme containing a molybdopterin cofactor, and two model compounds, I and II, which have pterin and quinoxaline, respectively, attached to a Cp2Mo[IV]-dithiolene chelate [Cp = cyclopentadienyl]. The effect of 34S incorporation was also determined. Several
L, Kilpatrick +6 more
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Crystal Structure of DMSO Reductase: Redox-Linked Changes in Molybdopterin Coordination
Science, 1996The molybdoenzyme dimethylsulfoxide (DMSO) reductase contributes to the release of dimethylsulfide, a compound that has been implicated in cloud nucleation and global climate regulation. The crystal structure of DMSO reductase from Rhodobacter sphaeroides reveals a monooxo molybdenum cofactor containing two ...
Schindelin, Hermann +4 more
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Geomicrobiology Journal, 2002
The dimethylsulfoxide (DMSO) reductase family of molybdenum enzymes is a large and diverse group that is found in bacteria and archaea. These enzymes are characterised by a bis(molybdopterin guanine dinucleotide)Mo form of the molybdenum cofactor, and they are particularly important in anaerobic respiration including the dissimilatory reduction of ...
Philip Hugenholtz +2 more
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The dimethylsulfoxide (DMSO) reductase family of molybdenum enzymes is a large and diverse group that is found in bacteria and archaea. These enzymes are characterised by a bis(molybdopterin guanine dinucleotide)Mo form of the molybdenum cofactor, and they are particularly important in anaerobic respiration including the dissimilatory reduction of ...
Philip Hugenholtz +2 more
exaly +5 more sources
Advances in Experimental Medicine and Biology, 2015
Protein folding and structure have been of interest since the dawn of protein chemistry. Following translation from the ribosome, a protein must go through various steps to become a functional member of the cellular society. Every protein has a unique function in the cell and is classified on this basis.
Raymond J Turner
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Protein folding and structure have been of interest since the dawn of protein chemistry. Following translation from the ribosome, a protein must go through various steps to become a functional member of the cellular society. Every protein has a unique function in the cell and is classified on this basis.
Raymond J Turner
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