Results 241 to 250 of about 202,224 (260)

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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Optical transitions of molybdenum(V) in glycerol-inhibited DMSO reductase from Rhodobacter sphaeroides

Inorganic Chemistry, 1993
Michael G. Finnegan, James Hilton, K. V. Rajagopalan, Michael K. Johnson   +3 more
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Few physicians prescribe 5-alpha reductase inhibitors for prostate cancer prevention†

Ca-A Cancer Journal for Clinicians, 2011
Mary Kay Barton
exaly  

Amperometric dimethyl sulfoxide sensor using dimethyl sulfoxide reductase from

Biosensors and Bioelectronics, 2003
Mitsuru Abo, Sunao Yamazaki, Akira Okubo
exaly  

Redox characteristics of the tungsten DMSO reductase of Rhodobacter capsulatus

FEBS Letters, 2003
Peter-Leon Hagedoorn, Wilfred R Hagen, Susan Bailey   +2 more
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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