Related ArticlesA simple protocol to study blue copper proteins by NMR.
Eur J Biochem. 2003 Feb;270(4):600-9
Authors: Gelis I, Katsaros N, Luchinat C, Piccioli M, Poggi L
In the case of oxidized plastocyanin from Synechocystis sp. PCC6803, an NMR approach based on classical two and three dimensional experiments for sequential assignment leaves unobserved 14 out of 98 amino acids. A protocol which simply makes use of tailored versions of 2D HSQC and 3D CBCA(CO)NH and CBCANH leads to the identification of nine of the above 14 residues. The proposed protocol differs from previous approaches in that it does not involve the use of unconventional experiments designed specifically for paramagnetic systems, and does not exploit the occurrence of a corresponding diamagnetic species in chemical exchange with the blue copper form. This protocol is expected to extend the popularity of NMR in the structural studies of copper (II) proteins, allowing researchers to increase the amount of information available via NMR on the neighborhood of a paramagnetic center without requiring a specific expertise in the field. The resulting 3D spectra are standard spectra that can be handled by any standard software for protein NMR data analysis.
A simple protocol for amino acid type selective isotope labeling in insect cells with improved yields and high reproducibility
A simple protocol for amino acid type selective isotope labeling in insect cells with improved yields and high reproducibility
Abstract An easy to use and robust approach for amino acid type selective isotope labeling in insect cells is presented. It relies on inexpensive commercial media and can be implemented in laboratories without sophisticated infrastructure. In contrast to previous protocols, where either high protein amounts or high incorporation ratios were obtained, here we achieve both at the same time. By supplementing media with a well considered amount of yeast extract,...
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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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[NMR paper] Metal-ligand interactions in perturbed blue copper sites: a paramagnetic (1)H NMR stu
Metal-ligand interactions in perturbed blue copper sites: a paramagnetic (1)H NMR study of Co(II)-pseudoazurin.
Related Articles Metal-ligand interactions in perturbed blue copper sites: a paramagnetic (1)H NMR study of Co(II)-pseudoazurin.
J Biol Inorg Chem. 2003 Jan;8(1-2):75-82
Authors: Fernández CO, Niizeki T, Kohzuma T, Vila AJ
Pseudoazurin is an electron transfer copper protein, a member of the cupredoxin family. The protein is frequently found in denitrifying bacteria, where it is the electron donor of nitrite reductase. The copper at...
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11-24-2010 08:58 PM
[NMR paper] Metal-ligand interplay in blue copper proteins studied by 1H NMR spectroscopy: Cu(II)
Metal-ligand interplay in blue copper proteins studied by 1H NMR spectroscopy: Cu(II)-pseudoazurin and Cu(II)-rusticyanin.
Related Articles Metal-ligand interplay in blue copper proteins studied by 1H NMR spectroscopy: Cu(II)-pseudoazurin and Cu(II)-rusticyanin.
J Am Chem Soc. 2002 Nov 20;124(46):13698-708
Authors: Donaire A, Jiménez B, Fernández CO, Pierattelli R, Niizeki T, Moratal JM, Hall JF, Kohzuma T, Hasnain SS, Vila AJ
The blue copper proteins (BCPs), pseudoazurin from Achromobacter cycloclastes and rusticyanin from Thiobacillus...
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11-24-2010 08:58 PM
[NMR paper] A general method for determining the electron self-exchange rates of blue copper prot
A general method for determining the electron self-exchange rates of blue copper proteins by longitudinal NMR relaxation.
Related Articles A general method for determining the electron self-exchange rates of blue copper proteins by longitudinal NMR relaxation.
J Am Chem Soc. 2002 Apr 17;124(15):4093-6
Authors: Jensen MR, Hansen DF, Led JJ
A general NMR method is presented that allows a precise determination of the second-order rate constant, k(ese), for the electron self-exchange in blue copper proteins, from the longitudinal relaxation...
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[NMR paper] Electronic characterization of the oxidized state of the blue copper protein rusticya
Electronic characterization of the oxidized state of the blue copper protein rusticyanin by 1H NMR: is the axial methionine the dominant influence for the high redox potential?
Related Articles Electronic characterization of the oxidized state of the blue copper protein rusticyanin by 1H NMR: is the axial methionine the dominant influence for the high redox potential?
Biochemistry. 2001 Jan 23;40(3):837-46
Authors: Donaire A, Jiménez B, Moratal J, Hall JF, Hasnain SS
The oxidized state of rusticyanin, the blue copper protein with the highest...
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11-19-2010 08:32 PM
[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, JimĂŠnez HR, Donaire A, Moratal JM
Substitution of copper by cobalt in blue copper proteins gives a paramagnetic metalloderivative...
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[NMR paper] Electrostatic recognition in redox copper proteins: a 1H NMR study of the protonation
Electrostatic recognition in redox copper proteins: a 1H NMR study of the protonation behavior of His 19 in oxidized and reduced Cu,Zn superoxide dismutase.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Electrostatic recognition in redox copper proteins: a 1H NMR study of the protonation behavior of His 19 in oxidized and reduced Cu,Zn superoxide dismutase.
Arch Biochem Biophys. 1993 Mar;301(2):244-50
Authors: Desideri A, Polticelli F, Falconi M, Sette M, Ciriolo MR, Paci M,...