Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Sergei V. Khangulov"'
Publikováno v:
Inorganic Chemistry. 39:3009-3019
Synthesis, solution structures, and electrochemistry of several dinuclear Mn2(II,II) complexes (1-4) and Mn2(III,III) complexes (6 and 8), derived from a functional catalase mimic [(L1,2)Mn2(II,II)(mu 13-O2CCH3)]2+ (1) are described that enable testi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0cee4019709b3857714fd5d084d331bf
https://doi.org/10.1021/ic9911769
https://doi.org/10.1021/ic9911769
Publikováno v:
Biochemistry. 37:8539-8550
Rat liver arginase contains a dimanganese(II,II) center per subunit that is required for catalytic hydrolysis of l-arginine to form urea and l-ornithine. A recent crystallographic study has shown that the Mn2 center consists of two coordinatively ine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::75bccde23ad9094ae25c4dd1f8ea9aff
https://doi.org/10.1021/bi972874c
https://doi.org/10.1021/bi972874c
Autor:
Jun Dong, Graham N. George, Robert A. Scott, Christopher M. Colangelo, and Vadim N. Gladyshev, Thressa C. Stadtman, Sergei V. Khangulov
Publikováno v:
Journal of the American Chemical Society. 120:1267-1273
X-ray absorption spectroscopy at the molybdenum and selenium K-edges has been used to probe the active site structure of Escherichia coli formate dehydrogenase H. The active sites of both oxidized and reduced wild-type protein, and of a variant conta
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7a025cae3efcdc3321113f58e7d27875
https://doi.org/10.1021/ja973004l
https://doi.org/10.1021/ja973004l
Autor:
T. M. Sossong, G. C. Dismukes, R. C. Cavalli, David E. Ash, Sergei V. Khangulov, Dianne Robert Soprano
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 2:433-443
Rat liver arginase contains a dinuclear Mn2(II,II) center in each subunit having EPR properties similar to those observed in Mn-catalases. The principal physiologic role of arginase is catalyzing the hydrolytic cleavage of l-arginine to produce l-orn
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::27516f9a79b5141a6692855e0db22c4e
https://doi.org/10.1007/s007750050154
https://doi.org/10.1007/s007750050154
Autor:
Thressa C. Stadtman, Peter D. Sun, Sergei V. Khangulov, Vadim N. Gladyshev, Jeffrey C. Boyington
Publikováno v:
Science. 275:1305-1308
Formate dehydrogenase H from Escherichia coli contains selenocysteine (SeCys), molybdenum, two molybdopterin guanine dinucleotide (MGD) cofactors, and an Fe 4 S 4 cluster at the active site and catalyzes the two-electron oxidation of formate to carbo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ee50e4f37705649b13ac3173a45b44eb
https://doi.org/10.1126/science.275.5304.1305
https://doi.org/10.1126/science.275.5304.1305
Autor:
Jeffrey C. Boyington, Thressa C. Stadtman, Vadim N. Gladyshev, David A. Grahame, Peter D. Sun, Sergei V. Khangulov
Publikováno v:
Journal of Biological Chemistry. 271:8095-8100
The selenocysteine-containing formate dehydrogenase H (FDH) is an 80-kDa component of the Escherichia coli formate-hydrogen lyase complex. The molybdenum-coordinated selenocysteine is essential for catalytic activity of the native enzyme. FDH in dilu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::74984c809440d2b1f84459e9147f5cb9
https://doi.org/10.1074/jbc.271.14.8095
https://doi.org/10.1074/jbc.271.14.8095
Publikováno v:
Proceedings of the National Academy of Sciences. 91:7708-7711
Formate dehydrogenase H from Escherichia coli contains multiple redox centers, which include a molybdopterin cofactor, an iron-sulfur center, and a selenocysteine residue (SeCys-140 in the polypeptide chain) that is essential for catalytic activity.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::244f6f87e1d40970738e11ede76815d4
https://doi.org/10.1073/pnas.91.16.7708
https://doi.org/10.1073/pnas.91.16.7708
Publikováno v:
Journal of the American Chemical Society. 116:891-897
Catalysts which functionally mimic the bacterial dimanganese catalase enzymes have been synthesized and their structure, electrochemical, redox, and EPR spectra have been compared to the enzyme. These compounds are formulated as [LMn 2 II,II X] Y 2 ,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::91140fb44874c3a0305b1db11272b362
https://doi.org/10.1021/ja00082a008
https://doi.org/10.1021/ja00082a008
Publikováno v:
Inorganic Chemistry. 33:382-387
A general approach for simulation of APR spectra of mixed-valence dimanganese complexes and proteins is presented, based on the theory of Sage et al. (J. Am. Chem. Soc. 1989, 111, 7239-7247), which overcomes limitations inherent in the theory of stro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7af932d3a1162905ae7af1a67345217a
https://doi.org/10.1021/ic00080a030
https://doi.org/10.1021/ic00080a030
Publikováno v:
Biochemistry. 32:4912-4924
The 1H hyperfine tensors of the dimanganese(III,IV) oxidation state of the non-heme-type catalase enzyme from the thermophilic bacterium Thermus thermophilus have been measured by electron nuclear double resonance (ENDOR) spectroscopy at pH 6.5-9. Th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::64298046b19557f9972b8179cdb5c3b2
https://doi.org/10.1021/bi00069a028
https://doi.org/10.1021/bi00069a028