Results 231 to 240 of about 202,224 (260)
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Environmental Science & Technology
The recently proposed partial denitrification (PD), terminating nitrate reduction to nitrite, has been regarded as a promising alternative to nitrite supplying for anammox bacteria. The most important aspect of the PD process for engineering application is the stable and continuous supply of nitrite.
Zhi-Bin Wang, Shou-Qing Ni, Taeho Lee
exaly +3 more sources
The recently proposed partial denitrification (PD), terminating nitrate reduction to nitrite, has been regarded as a promising alternative to nitrite supplying for anammox bacteria. The most important aspect of the PD process for engineering application is the stable and continuous supply of nitrite.
Zhi-Bin Wang, Shou-Qing Ni, Taeho Lee
exaly +3 more sources
JBIC Journal of Biological Inorganic Chemistry, 2018
We have examined the kinetic and spectroscopic properties of a tungsten-substituted form of DMSO reductase from Rhodobacter sphaeroides, an enzyme that normally possesses molybdenum. Partial reduction with sodium dithionite yields a well-resolved W(V) EPR signal of the so-called "high-g split" type that exhibits markedly greater g-anisotropy than the ...
Josué, Pacheco +2 more
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We have examined the kinetic and spectroscopic properties of a tungsten-substituted form of DMSO reductase from Rhodobacter sphaeroides, an enzyme that normally possesses molybdenum. Partial reduction with sodium dithionite yields a well-resolved W(V) EPR signal of the so-called "high-g split" type that exhibits markedly greater g-anisotropy than the ...
Josué, Pacheco +2 more
openaire +2 more sources
ArxA, a new clade of arsenite oxidase within the DMSO reductase family of molybdenum oxidoreductases
Environmental Microbiology, 2012Summary 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 +8 more
openaire +2 more sources
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 +5 more
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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 +5 more
openaire +2 more sources
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 +4 more
openaire +1 more source
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 +4 more
openaire +1 more source
Vibrational spectroscopic study on the bis-MGD cofactor in DMSO reductase enzymes
2023In 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.
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Bioorganic & Medicinal Chemistry, 1995
The substrate specificity and enantioselectivity of DMSO reductase from Rhodobacter sphaeroides f.s. denitrificans were studied on a series of alkyl aryl sulfoxides as substrate. The enzyme was found to catalyze deoxygenation of (S)-sulfoxides predominantly. (R)-Sulfoxides were recovered with a high enantiomeric excess.
M, Abo +3 more
openaire +2 more sources
The substrate specificity and enantioselectivity of DMSO reductase from Rhodobacter sphaeroides f.s. denitrificans were studied on a series of alkyl aryl sulfoxides as substrate. The enzyme was found to catalyze deoxygenation of (S)-sulfoxides predominantly. (R)-Sulfoxides were recovered with a high enantiomeric excess.
M, Abo +3 more
openaire +2 more sources
Dendrimer Encapsulation of [MoVOS4] Cores: Implications for the DMSO Reductase Family of Enzymes
Inorganic Chemistry, 2000Recent crystal structures of DMSO reductases show that the active site is deeply buried inside the protein matrix.
S, Mondal, P, Basu
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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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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
openaire +2 more sources