Zobrazeno 1 - 10
of 459
pro vyhledávání: '"K.V. Rajagopalan"'
Publikováno v:
Biochemistry. 51:1134-1147
Eukaryotic sulfite oxidase is a dimeric protein that contains the molybdenum cofactor and catalyzes the metabolically essential conversion of sulfite to sulfate as the terminal step in the metabolism of cysteine and methionine. Nitrate reductase is a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::db5b57cc92e9e7ea8e499a2b21e3ea05
https://doi.org/10.1021/bi201206v
https://doi.org/10.1021/bi201206v
Publikováno v:
Inorganic Chemistry. 50:9406-9413
Valuable information on the active sites of molybdenum enzymes has been provided from both Mo(V) electron paramagnetic resonance (EPR) spectroscopy and X-ray absorption spectroscopy (XAS). One of three major categories of Mo(V) EPR signals from the m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae5617e75e9ac0d77a7a84981a8a3184
https://doi.org/10.1021/ic201030u
https://doi.org/10.1021/ic201030u
Publikováno v:
Thermochimica Acta. :21-26
The interaction between uranyl nitrate hexahydrate (UNH) and rubidium nitrate in solid state at elevated temperatures has been studied for several compositions using simultaneous thermal analysis techniques (TG–DTA–EGA), X-ray diffraction and IR
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6256d8febbaafc09bfe86bbf318e09c1
https://doi.org/10.1016/j.tca.2010.04.024
https://doi.org/10.1016/j.tca.2010.04.024
Publikováno v:
Journal of Nuclear Materials. 393:497-503
Solid state reactions between uranyl nitrate hexahydrate and nickel nitrate hexahydrate in mixtures of various ratios have been studied at elevated temperatures. The binary system of uranyl nitrate hexahydrate and nickel nitrate hexahydrate was found
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1b2f2d62806333f8976eeaf7519667b7
https://doi.org/10.1016/j.jnucmat.2009.07.011
https://doi.org/10.1016/j.jnucmat.2009.07.011
Autor:
K.V. Rajagopalan
Publikováno v:
Nutrition Reviews. 45:321-328
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c5d96e6c915e62e99a9c544916a220a
https://doi.org/10.1111/j.1753-4887.1987.tb00981.x
https://doi.org/10.1111/j.1753-4887.1987.tb00981.x
Autor:
K.V. Rajagopalan, Changjian Feng, Andrei V. Astashkin, John H. Enemark, Eric L. Klein, Kayunta Johnson-Winters, Heather L. Wilson, Arnold M. Raitsimring
Publikováno v:
Journal of the American Chemical Society. 130:8471-8480
Electron paramagnetic resonance (EPR) investigation of the Mo(V) center of the pathogenic R160Q mutant of human sulfite oxidase (hSO) confirms the presence of three distinct species whose relative abundances depend upon pH. Species 1 is exclusively p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3726e5e6062937a9dc8eef83ebb34bfe
https://doi.org/10.1021/ja801406f
https://doi.org/10.1021/ja801406f
Autor:
Arnold M. Raitsimring, Andrei V. Astashkin, Heather L. Wilson, K.V. Rajagopalan, Changjian Feng, John H. Enemark
Publikováno v:
Inorganica Chimica Acta. 361:941-946
The Mo(V) forms of the Tyr343Phe (Y343F) mutant of human sulfite oxidase (SO) have been investigated by continuous wave (CW) and variable frequency pulsed EPR spectroscopies as a function of pH. The CW EPR spectrum recorded at low pH (∼6.9) has g-v
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c7749d4e793e1ad877f1aadaaf92549f
https://doi.org/10.1016/j.ica.2007.05.023
https://doi.org/10.1016/j.ica.2007.05.023
Publikováno v:
Inorganic Chemistry. 47:1074-1078
We report a structural characterization of the molybdenum site of recombinant Escherichia coli trimethylamine N-oxide (TMAO) reductase using X-ray absorption spectroscopy. The enzyme active site shows considerable similarity to that of dimethyl sulfo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::65e27bb050028ced1843d379085d3448
https://doi.org/10.1021/ic701956f
https://doi.org/10.1021/ic701956f
Publikováno v:
Biochemistry. 47:615-626
In almost all biological life forms, molybdenum and tungsten are coordinated by molybdopterin (MPT), a tricyclic pyranopterin containing a cis-dithiolene group. Together, the metal and the pterin moiety form the redox reactive molybdenum cofactor (Mo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::16fe7de746adbc818ab0f5991a612174
https://doi.org/10.1021/bi701734g
https://doi.org/10.1021/bi701734g
Publikováno v:
Biochemistry. 46:909-916
In Escherichia coli, the MoaD protein plays a central role in the conversion of precursor Z to molybdopterin (MPT) during molybdenum cofactor biosynthesis. MoaD has a fold similar to that of ubiquitin and contains a highly conserved C-terminal Gly-Gl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a202ef891951d99fc86a3e949df5c7ba
https://doi.org/10.1021/bi062011w
https://doi.org/10.1021/bi062011w