Results 211 to 220 of about 202,224 (260)

Metal thiosemicarbazonates as dual mR2 RNR and colchicine-site tubulin inhibitors: from biochemical inhibition to mitotic arrest in MCF-7 breast cancer cells.

Inorg Chem Front
Palamarciuc O, Ciubotaru BI, Stoica AC, Hejl M, Hammerstad M, Balan-Porcarasu M, Shova S, Gátszegi GT, Popović Bijelić A, Reynisson J, Jakupec MA, Zalibera M, Rapta P, Enyedy ÉA, Peptanariu D, Dascalu M, Cazacu M, Hamel E, Arion VB.   +18 more
europepmc   +1 more source

The high resolution crystal structure of DMSO reductase in complex with DMSO

Journal of Molecular Biology, 1998
The crystal structure of the molybdenum enzyme dimethylsulphoxide reductase (DMSOR) has been determined at 1.9 Å resolution with substrate bound at the active site.
Alastair G McEwan, S Bailey
exaly   +7 more sources

DmsD is required for the biogenesis of DMSO reductase in Escherichia coli but not for the interaction of the DmsA signal peptide with the Tat apparatus

FEBS Letters, 2003
The DmsD protein is essential for the biogenesis of DMSO reductase in Escherichia coli, and binds the signal peptide of the DmsA subunit, a Tat substrate. This suggests a role as a guidance factor to target pre-DmsA to the translocase.
Colin Robinson, Raymond J Turner
exaly   +5 more sources

Isolation and characterisation of bacterial strains containing enantioselective DMSO reductase activity: application to the kinetic resolution of racemic sulfoxides

Applied Microbiology and Biotechnology, 2004
The kinetic resolution of racemic sulfoxides by dimethyl sulfoxide (DMSO) reductases was investigated with a range of microorganisms. Three bacterial isolates (provisionally identified as Citrobacter braakii, Klebsiella sp.
Howard Dalton, Narain D Sharma, Robert A Holt   +2 more
exaly   +6 more sources

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Emerging Chemical Diversity and Potential Applications of Enzymes in the DMSO Reductase Superfamily

Annual Review of Biochemistry, 2022
Molybdenum- and tungsten-dependent proteins catalyze essential processes in living organisms and biogeochemical cycles. Among these enzymes, members of the dimethyl sulfoxide (DMSO) reductase superfamily are considered the most diverse, facilitating a wide range of chemical transformations that can be categorized as oxygen atom installation, removal ...
Emily Balskus, Minwoo Bae
exaly   +3 more sources

Effect of the protein ligand in DMSO reductase studied by computational methods [PDF]

Journal of Inorganic Biochemistry, 2017
The DMSO reductase family is the largest and most diverse family of mononuclear molybdenum oxygen-atom-transfer proteins. Their active sites contain a Mo ion coordinated to two molybdopterin ligands, one oxo group in the oxidised state, and one additional, often protein-derived ligand.
Ulf Ryde, Geng Dong
exaly   +4 more sources