Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Gnana S. Siluvai"'
Publikováno v:
Inorganica Chimica Acta. 388:46-51
Two dinuclear trivalent cobalt complexes viz. [Co2(P1–O)(AcO)(H2O)(OH)](ClO4)3, (1) and [Co2(P1–O)(AcO)(DPP)](ClO4)3, (2), where P 1 – O = N , N ′ , N ″ , N ‴ -tetrakis ( 2 -methylpyridyl ) - 2 -hydroxy- 1 , 3 -diaminopropane , AcO = acet
Autor:
Mary B. Mayfield, Gnana S. Siluvai, Serena DeBeer George, Ninian J. Blackburn, Mark J. Nilges
Publikováno v:
Journal of the American Chemical Society. 132:5215-5226
Sco is a mononuclear red copper protein involved in the assembly of cytochrome c oxidase. It is spectroscopically similar to red copper nitrosocyanin, but unlike the latter, which has one copper cysteine thiolate, the former has two. In addition to t
Autor:
Narasimha N. Murthy, Gnana S. Siluvai
Publikováno v:
Polyhedron. 28:2149-2156
μ-1,3-Acetamide or acetate bridged, symmetric and asymmetric dicopper(II) complexes viz [Cu2(P1-O−)(NHAc−)](ClO4)2 (1), [Cu2(P2-O−)(OAc−)](ClO4)2 (2) and [Cu2(P2′-O−)(OAc−)(H2O)](ClO4)2 (3) were synthesized by employing classic dinucle
Publikováno v:
Angewandte Chemie International Edition. 47:9084-9087
The beta bind: Copper(I) binds to amyloid {beta}-peptide fragments (see structure) as a stable bis(histidine), two-coordinate, near-linear complex, even in the presence of potential additional ligands. As has been proposed or assumed in other studies
Publikováno v:
IndraStra Global.
A dinuclear copper(II) complex [Cu 2(PD)(DPP -) 2](ClO 4) 2 (1) incorporating a constrained binucleating hexadenate ligand, PD (1,3-bis{bis[(2-pyridyl)ethyl]amino}benzene), and coligand, DPP - (diphenylphosphate) was synthesized and characterized, wi
Publikováno v:
Biochemistry. 48(51)
Sco-like proteins contain copper bound by two cysteines and a histidine residue. Although their function is still incompletely understood, there is a clear involvement with the assembly of cytochrome oxidases that contain the Cu(A) center in subunit
Autor:
Gnana S. Siluvai, Vinzenz M. Unger, Ninian J. Blackburn, Christopher J. De Feo, Stephen G. Aller
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 106(11)
Copper uptake proteins (CTRs), mediate cellular acquisition of the essential metal copper in all eukaryotes. Here, we report the structure of the human CTR1 protein solved by electron crystallography to an in plane resolution of 7 Å. Reminiscent of
Autor:
Stephen G. Aller, Vinzenz M. Unger, Maya Shcushan, Nir Ben-Tal, Yariv Barkan, Christopher J. De Feo, Ninian J. Blackburn, Gnana S. Siluvai
Publikováno v:
Biophysical Journal. 96(3)
Copper uptake proteins (CTRs), mediate cellular acquisition of the essential metal copper in all eukaryotes. Using electron cryomicroscopy, we determined a 3D-structure of hCTR1 at ∼7A resolution. The structure suggests that CTR1 proteins transport
Autor:
Narasimha N. Murthy, Gnana S. Siluvai
Publikováno v:
IndraStra Global.
Two dinuclear spin-coupled divalent cobalt complexes, [Co 2 (P1-O)(μ 2 -OAc)](ClO 4 ) 2 , ( 1 ) and [Co 2 (P1-O)(μ 2 -BNPP)](ClO 4 ) 2 , ( 2 ) containing μ-1,3 acetate (OAc) and bis(4-nitrophenyl)phosphate (BNPP) auxiliary bridges, respectively, w
Publikováno v:
Biochemistry. 46(42)
Copper binding and X-ray aborption spectroscopy studies are reported on untagged human CCS (hCCS; CCS = copper chaperone for superoxide dismutase) isolated using an intein self-cleaving vector and on single and double Cys to Ala mutants of the hCCS M