Related ArticlesX-ray absorption and NMR spectroscopic studies of CopZ, a copper chaperone in Bacillus subtilis: the coordination properties of the copper ion.
Biochemistry. 2003 Mar 4;42(8):2467-74
Authors: Banci L, Bertini I, Del Conte R, Mangani S, Meyer-Klaucke W
XAS studies have been performed, under various experimental conditions, on a copper(I)-transporting protein, CopZ, of Bacillus subtilis. The copper(I) ion, reduced with dithiothreitol, is three-coordinate with three sulfur donor atoms, two of which presumably provided by the protein and one by dithiothreitol. If a molar excess of acetate (15 mM; 5:1 respect to CopZ) or citrate (6 mM; 2:1 respect to CopZ) is present in solution, the EXAFS spectra suggest the presence of a dimeric form involving a close contact between Cu(I) ions from two molecules, where Cu is still three-coordinate. (1)H and (15)N NMR data provide further structural details. If copper reduction is accomplished with ascorbate, the data indicate that one oxygen of ascorbate enters in the first-coordination sphere of copper, together with two sulfur atoms, in a dimeric form of the protein. These results are instructive and have been discussed with respect to the molecular basis of copper trafficking.
Probing the Interaction of Cisplatin with the Human Copper Chaperone Atox1 by Solution and In-Cell NMR Spectroscopy
Probing the Interaction of Cisplatin with the Human Copper Chaperone Atox1 by Solution and In-Cell NMR Spectroscopy
Fabio Arnesano, Lucia Banci, Ivano Bertini, Isabella C. Felli, Maurizio Losacco and Giovanni Natile
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja207346p/aop/images/medium/ja-2011-07346p_0003.gif
Journal of the American Chemical Society
DOI: 10.1021/ja207346p
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/9nWkAzWuq20
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[NMR paper] A NMR study of the interaction of a three-domain construct of ATP7A with copper(I) and copper(I)-HAH1: the interplay of domains.
A NMR study of the interaction of a three-domain construct of ATP7A with copper(I) and copper(I)-HAH1: the interplay of domains.
Related Articles A NMR study of the interaction of a three-domain construct of ATP7A with copper(I) and copper(I)-HAH1: the interplay of domains.
J Biol Chem. 2005 Nov 18;280(46):38259-63
Authors: Banci L, Bertini I, Cantini F, Chasapis CT, Hadjiliadis N, Rosato A
ATP7A is a P-type ATPase involved in copper(I) homeostasis in humans. It possesses a long N-terminal tail protruding into the cytosol and containing six...
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12-01-2010 06:56 PM
[NMR paper] An NMR study of the interaction between the human copper(I) chaperone and the second
An NMR study of the interaction between the human copper(I) chaperone and the second and fifth metal-binding domains of the Menkes protein.
Related Articles An NMR study of the interaction between the human copper(I) chaperone and the second and fifth metal-binding domains of the Menkes protein.
FEBS J. 2005 Feb;272(3):865-71
Authors: Banci L, Bertini I, Ciofi-Baffoni S, Chasapis CT, Hadjiliadis N, Rosato A
The interaction between the human copper(I) chaperone, HAH1, and one of its two physiological partners, the Menkes disease protein...
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11-24-2010 11:14 PM
[NMR paper] NMR spin-echo studies of hydration properties of the molecular chaperone alpha-crysta
NMR spin-echo studies of hydration properties of the molecular chaperone alpha-crystallin in the bovine lens.
Related Articles NMR spin-echo studies of hydration properties of the molecular chaperone alpha-crystallin in the bovine lens.
Biochim Biophys Acta. 2002 Jul 29;1598(1-2):46-54
Authors: Babizhayev MA, Nikolayev GN, Goryachev SN, Bours J
The water-binding properties of bovine lens alpha-crystallin, collagen from calf skin and bovine serum albumin (BSA), were investigated with various techniques. The water absorptive capacity was...
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11-24-2010 08:58 PM
[NMR paper] NMR structure and metal interactions of the CopZ copper chaperone.
NMR structure and metal interactions of the CopZ copper chaperone.
Related Articles NMR structure and metal interactions of the CopZ copper chaperone.
J Biol Chem. 1999 Aug 6;274(32):22597-603
Authors: Wimmer R, Herrmann T, Solioz M, Wüthrich K
A recently discovered family of proteins that function as copper chaperones route copper to proteins that either require it for their function or are involved in its transport. In Enterococcus hirae the copper chaperone function is performed by the 8-kDa protein CopZ. This paper describes the NMR...
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11-18-2010 08:31 PM
[NMR paper] NMR spectroscopic studies of the hydrogenosomal [2Fe-2S] ferredoxin from Trichomonas
NMR spectroscopic studies of the hydrogenosomal ferredoxin from Trichomonas vaginalis: hyperfine-shifted 1H resonances.
Related Articles NMR spectroscopic studies of the hydrogenosomal ferredoxin from Trichomonas vaginalis: hyperfine-shifted 1H resonances.
J Inorg Biochem. 1998 Dec;72(3-4):127-31
Authors: Liu HY, Germanas JP
The hyperfine-shifted 1H NMR resonances of oxidized and reduced Trichomonas vaginalis ferredoxin, a functionally unique ferredoxin, have been studied. The oxidized protein spectrum displayed a pattern of six broad...
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11-17-2010 11:15 PM
[NMR paper] 1H NMR spectroscopic studies on the interactions between human plasma antithrombin II
1H NMR spectroscopic studies on the interactions between human plasma antithrombin III and defined low molecular weight heparin fragments.
Related Articles 1H NMR spectroscopic studies on the interactions between human plasma antithrombin III and defined low molecular weight heparin fragments.
Biochemistry. 1992 Mar 3;31(8):2286-94
Authors: Horne A, Gettins P
The effects of length and composition upon the antithrombin-binding properties of heparin have been investigated for two series of structurally related heparin oligosaccharides. Each...
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[NMR paper] 1H NMR studies of reactions of copper complexes with human blood plasma and urine.
1H NMR studies of reactions of copper complexes with human blood plasma and urine.
Related Articles 1H NMR studies of reactions of copper complexes with human blood plasma and urine.
Biochem Pharmacol. 1992 Jan 22;43(2):137-45
Authors: Bligh SW, Boyle HA, McEwen AB, Sadler PJ, Woodham RH
Reactions of the copper complexes Cu(II)Cl2, 2-, and + (where DIPS is 3,5-diisopropylsalicylate and DMP is 2,9-dimethylphenanthroline) with human blood plasma and urine have been studied by 500 MHz 1H NMR spectroscopy, and CD spectroscopy has been used to...