Results 201 to 210 of about 35,348 (219)

Synthesis and Structures of Bis(dithiolene)molybdenum Complexes Related to the Active Sites of the DMSO Reductase Enzyme Family

Inorganic Chemistry, 1999
Structural analogues of the reduced (Mo(IV)) sites of members of the DMSO reductase family of molybdoenzymes are sought. These sites usually contain two pterin-dithiolene cofactor ligands and one protein-based ligand. Reaction of [Mo(MeCN)3(CO)3] and [Ni(S2C2R2)2] affords the trigonal prismatic complexes [Mo(CO)2(S2C2R2)2] (R = Me (1), Ph (2)), which ...
B S, Lim, J P, Donahue, R H, Holm
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Interaction of an Engineered [3Fe-4S] Cluster with a Menaquinol Binding Site of Escherichia coli DMSO Reductase

Biochemistry, 1996
We have characterized by EPR the interaction of the Em,7 = -50 mV [4Fe-4S] cluster of Escherichia coli DMSO reductase (DmsABC) with a menaquinol (MQH2) binding site. Potentiometric titrations indicate that in DmsAB(C102S)C, the Em,7 = -50 mV [4Fe-4S] cluster is replaced by an Em,7 = +260 mV [3Fe-4S] cluster.
R A, Rothery, J H, Weiner
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Topological characterization of Escherichia coli DMSO reductase by electron paramagnetic resonance spectroscopy of an engineered iron-sulfur [3Fe-4S] cluster

Biochemistry, 1993
We have applied the technique of distance estimations using the exogenous paramagnetic probe dysprosium (III) complexed with EDTA (DyEDTA) to study the topology of Escherichia coli dimethyl sulfoxide reductase (DmsABC) in situ in cytoplasmic membrane and whole cell preparations. The electron transfer subunit (DmsB) of this enzyme contains four [4Fe-4S]
R A, Rothery, J H, Weiner
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The Oxo-Gate Hypothesis and DMSO Reductase:  Implications for a Psuedo-σ Bonding Interaction Involved in Enzymatic Electron Transfer

Inorganic Chemistry, 2000
The electronic structure of (PPh4)[MoO(benzene-1,2-dithiolate)2], a paramagnetic analogue of the oxidized active site of DMSO reductase, has been investigated by electronic absorption, magnetic circular dichroism, and resonance Raman spectroscopies. A pseudo-σ bonding interaction exists between the Mo dxy redox orbital and in-plane dithiolate orbitals,
Rebecca L. McNaughton, Matthew E. Helton, Nick D. Rubie, Martin L. Kirk   +3 more
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Structural and mechanistic investigations into Dimethylsulfide dehyddrogenase from Rhodovulum sulfidophilum; a moyybdoenzyme from the DMSO reductase family

Dimethyl sulfide (DMS) dehydrogenase from the purple non-sulfur bacterialspecies Rhodovulum (R.) suljidophilum is a heterotrimeric enzyme containing amolybdenum ion at its active centre, as well as five iron-sulfur clusters and a heme bcofactor. It is a Type II member of the dimethyl sulfoxide (DMSO) reductase family andcatalytically oxidizes DMS in ...
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The optical transitions of Mo(V) in glycerol-inhibited DMSO reductase from Rhodobacter sphaeroides

Journal of Inorganic Biochemistry, 1993
M.G. Finnegan, J. Hilton, K.V. Rajagopalan, M.K. Johnson   +3 more
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The high resolution crystal structure of DMSO reductase in complex with DMSO 1 1Edited by D. C. Rees

Journal of Molecular Biology, 1998
Alastair Mcewan
exaly  

DmsD is required for the biogenesis of DMSO reductase inEscherichia colibut not for the interaction of the DmsA signal peptide with the Tat apparatus

FEBS Letters, 2003
Raymond J Turner
exaly  

Faculty Opinions recommendation of Kinetic consequences of the endogenous ligand to molybdenum in the DMSO reductase family: a case study with periplasmic nitrate reductase.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature, 2021
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Analysis of substrates for DMSO reductase from escherichia coli

1998
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