Related Articles113Cd-NMR investigation of a cadmium-substituted copper, zinc-containing superoxide dismutase from yeast.
Eur J Biochem. 1991 Jun 15;198(3):607-11
Authors: Kofod P, Bauer R, Danielsen E, Larsen E, Bjerrum MJ
113Cd nuclear magnetic resonance spectroscopy has been used to investigate the metal binding sites of cadmium-substituted copper, zinc-containing superoxide dismutase from baker's yeast. NMR signals were obtained for 113Cd(II) at the Cu site as well as for 113Cd(II) at the Zn site. The two subunits in the dimeric enzyme were found to have identical coordination properties towards 113Cd(II) at the Zn site when no copper is coordinated at the Cu site, and when Cu(I) or Cd(II) is coordinated, were found to be very small indicating that 113Cd(II) must be bound to the same number and type of ligands in both cases. Furthermore, the spectra show that the rate of exchange of protein-bound 113Cd(II) and free 113Cd2+ is slow on the NMR time scale also at the Cu site. The present study suggests an explanation for the discrepancy in the literature regarding 113Cd-NMR investigations of bovine superoxide dismutase.
Solution-state NMR structure and biophysical characterization of zinc-substituted rubredoxin B (Rv3250c) from Mycobacterium tuberculosis.
Solution-state NMR structure and biophysical characterization of zinc-substituted rubredoxin B (Rv3250c) from Mycobacterium tuberculosis.
Solution-state NMR structure and biophysical characterization of zinc-substituted rubredoxin B (Rv3250c) from Mycobacterium tuberculosis.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Sep 1;67(Pt 9):1148-53
Authors: Buchko GW, Hewitt SN, Napuli AJ, Van Voorhis WC, Myler PJ
Abstract
Owing to the evolution of multi-drug-resistant and extremely drug-resistant Mycobacterium tuberculosis strains,...
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[NMR paper] Crystallographic and NMR investigation of cobalt-substituted amicyanin.
Crystallographic and NMR investigation of cobalt-substituted amicyanin.
Related Articles Crystallographic and NMR investigation of cobalt-substituted amicyanin.
Biochemistry. 2004 Jul 27;43(29):9381-9
Authors: Carrell CJ, Wang X, Jones L, Jarrett WL, Davidson VL, Mathews FS
Cobalt(II) amicyanin was prepared by replacing the copper of the type I copper protein amicyanin from Paracoccus denitrificans with cobalt. The structure of the protein and the metal center have been characterized by X-ray crystallography and paramagnetic NMR spectroscopy....
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[NMR paper] Dynamic properties of the G93A mutant of copper-zinc superoxide dismutase as detected
Dynamic properties of the G93A mutant of copper-zinc superoxide dismutase as detected by NMR spectroscopy: implications for the pathology of familial amyotrophic lateral sclerosis.
Related Articles Dynamic properties of the G93A mutant of copper-zinc superoxide dismutase as detected by NMR spectroscopy: implications for the pathology of familial amyotrophic lateral sclerosis.
Biochemistry. 2003 Feb 25;42(7):1890-9
Authors: Shipp EL, Cantini F, Bertini I, Valentine JS, Banci L
The backbone assignment of the copper-zinc superoxide dismutase...
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Oxidation of Histidine Residues in Copper-Zinc Superoxide Dismutase by Bicarbonate-St
Oxidation of Histidine Residues in Copper-Zinc Superoxide Dismutase by Bicarbonate-Stimulated Peroxidase and Thiol Oxidase Activities: Pulse EPR and NMR Studies
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi1010305/aop/images/medium/bi-2010-010305_0006.gif
Biochemistry
DOI: 10.1021/bi1010305
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[NMR paper] 1H-NMR study of a cobalt-substituted blue copper protein: Pseudomonas aeruginosa Co(I
1H-NMR study of a cobalt-substituted blue copper protein: Pseudomonas aeruginosa Co(II)-azurin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles 1H-NMR study of a cobalt-substituted blue copper protein: Pseudomonas aeruginosa Co(II)-azurin.
Eur J Biochem. 1995 Jul 15;231(2):358-69
Authors: Salgado J, Jiménez HR, Donaire A, Moratal JM
Substitution of copper by cobalt in blue copper proteins gives a paramagnetic metalloderivative...
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[NMR paper] Copper- and silver-substituted yeast metallothioneins: sequential 1H NMR assignments
Copper- and silver-substituted yeast metallothioneins: sequential 1H NMR assignments reflecting conformational heterogeneity at the C terminus.
Related Articles Copper- and silver-substituted yeast metallothioneins: sequential 1H NMR assignments reflecting conformational heterogeneity at the C terminus.
Biochemistry. 1993 Jul 6;32(26):6773-87
Authors: Narula SS, Winge DR, Armitage IM
Complete 1H NMR sequential assignments have been made for copper(I)- and silver (I)-substituted metallothionein (MT) from Saccharomyces cerevisiae using standard...
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[NMR paper] Binding of cadmium(II) and zinc(II) to human and dog serum albumins. An equilibrium d
Binding of cadmium(II) and zinc(II) to human and dog serum albumins. An equilibrium dialysis and 113Cd-NMR study.
Related Articles Binding of cadmium(II) and zinc(II) to human and dog serum albumins. An equilibrium dialysis and 113Cd-NMR study.
Biochem Cell Biol. 1991 Dec;69(12):809-20
Authors: Goumakos W, Laussac JP, Sarkar B
The binding of Cd(II) and Zn(II) to human serum albumin (HSA) and dog serum albumin (DSA) has been studied by equilibrium dialysis and 113Cd(II)-NMR techniques at physiological pH. Scatchard analysis of the equilibrium...
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[NMR paper] Binding of cadmium(II) and zinc(II) to human and dog serum albumins. An equilibrium d
Binding of cadmium(II) and zinc(II) to human and dog serum albumins. An equilibrium dialysis and 113Cd-NMR study.
Related Articles Binding of cadmium(II) and zinc(II) to human and dog serum albumins. An equilibrium dialysis and 113Cd-NMR study.
Biochem Cell Biol. 1991 Dec;69(12):809-20
Authors: Goumakos W, Laussac JP, Sarkar B
The binding of Cd(II) and Zn(II) to human serum albumin (HSA) and dog serum albumin (DSA) has been studied by equilibrium dialysis and 113Cd(II)-NMR techniques at physiological pH. Scatchard analysis of the equilibrium...