Results 191 to 200 of about 35,348 (219)

The nature and function of the catalytic centres of the DMSO reductases

Dalton Transactions, 2005
Density 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 ...
McNamara, Jonathan P., Hillier, Ian H., Bhachu, Tarnjeet S., Garner, C. David   +3 more
openaire   +2 more sources

Dithiolene coordination in the molybdopterin cofactor of DMSO reductase: in situ evidence from resonance Raman spectroscopy

Journal of the American Chemical Society, 1990
K V Rajagopalan
exaly   +2 more sources

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

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, Jennifer M. McGarry, Daniel J. Bain, Partha Basu   +3 more
openaire   +2 more sources

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(V) complexes.
Hanson, Graeme R., Ian Lane
openaire   +4 more sources

Crystal Structure of DMSO Reductase: Redox-Linked Changes in Molybdopterin Coordination

Science, 1996
The 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, Kisker, Caroline, Hilton, James, Rajagopalan, K. V., Rees, Douglas C.   +4 more
openaire   +3 more sources

ArxA, a new clade of arsenite oxidase within the DMSO reductase family of molybdenum oxidoreductases

Environmental Microbiology, 2012
Summary Arsenotrophy, growth coupled to autotrophic arsenite oxidation or arsenate respiratory reduction, occurs only in the prokaryotic domain of life. The enzymes responsible for arsenotrophy belong to distinct clades within the DMSO reductase family of molybdenum‐containing oxidoreductases: specifically ...
Kamrun, Zargar, Alison, Conrad, David L, Bernick, Todd M, Lowe, Viktor, Stolc, Shelley, Hoeft, Ronald S, Oremland, John, Stolz, Chad W, Saltikov   +8 more
openaire   +2 more sources

Geometric Control of Reduction Potential in Oxomolybdenum Centers:  Implications to the Serine Coordination in DMSO Reductase

Inorganic Chemistry, 2001
Two isomers (cis and trans) of (L1O)MoOCl2 have been synthesized and separated using the heteroscorpinate ligand L1OH, which possesses an N2O donor set.
S R, Davie, N D, Rubie, B S, Hammes, C J, Carrano, M L, Kirk, P, Basu   +5 more
openaire   +2 more sources

ChemInform Abstract: Electrochemical Enzymatic Deoxygenation of Chiral Sulfoxides Utilizing DMSO Reductase.

ChemInform, 2000
AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 100 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a “Full Text” option. The original article is trackable via the “References” option.
Mitsuru Abo, Makiko Dejima, Fumioki Asano, Akira Okubo, Sunao Yamazaki   +4 more
openaire   +1 more source

Vibrational spectroscopic study on the bis-MGD cofactor in DMSO reductase enzymes

2023
In nature, highly selective and efficient enzymes have been evolved to catalyze a wide variety of fundamental reactions at very low overpotentials. These enzymes can work under various conditions, i.a. different catalytic activities, in the presence of oxygen, specific bias or at very high temperatures.
openaire   +1 more source

Dendrimer Encapsulation of [Mo^VOS₄] Cores:  Implications for the DMSO Reductase Family of Enzymes

Inorganic Chemistry, 2000
Recent crystal structures of DMSO reductases show that the active site is deeply buried inside the protein matrix.
S, Mondal, P, Basu
openaire   +2 more sources