Related ArticlesMetal-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 the active site is coordinated to His40, Cys78, His81 and Met86 in a distorted tetragonal geometry. We have recorded and assigned the (1)H NMR spectra of Co(II)-substituted pseudoazurin from Achromobacter cycloclastes. The (1)H NMR spectrum of Co(II)-pseudoazurin closely resembles that of Co(II)-rusticyanin, reflecting an altered conformation for the Met-Co(II)-Cys moiety in both proteins, compared to Co(II)-azurin, amicyanin and stellacyanin. The electron spin density onto the Sgamma(Cys) is larger in Co(II)-pseudoazurin compared to Co(II)-rusticyanin. Instead, the Co(II)-Met interaction is similar in both derivatives. Hence, the different metal-ligand interactions might be independently modulated by the protein structure. The present work also shows that the electron spin density onto the Co(II)-S(cys) bond is sensibly smaller than the Cu(II)-S(cys). Notwithstanding, NMR data on Co(II)-substituted blue copper proteins can be safely extrapolated to native Cu(II) proteins.
[NMR paper] Metal binding sites in proteins: identification and characterization by paramagnetic NMR relaxation.
Metal binding sites in proteins: identification and characterization by paramagnetic NMR relaxation.
Related Articles Metal binding sites in proteins: identification and characterization by paramagnetic NMR relaxation.
Biochemistry. 2005 Aug 23;44(33):11014-23
Authors: Jensen MR, Petersen G, Lauritzen C, Pedersen J, Led JJ
A method is presented that allows the identification and quantitative characterization of metal binding sites in proteins using paramagnetic nuclear magnetic resonance spectroscopy. The method relies on the nonselective...
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[NMR paper] A simple protocol to study blue copper proteins by NMR.
A simple protocol to study blue copper proteins by NMR.
Related Articles A 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...
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[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] Axial ligand modulation of the electronic structures of binuclear copper sites: analy
Axial ligand modulation of the electronic structures of binuclear copper sites: analysis of paramagnetic 1H NMR spectra of Met160Gln Cu(A).
Related Articles Axial ligand modulation of the electronic structures of binuclear copper sites: analysis of paramagnetic 1H NMR spectra of Met160Gln Cu(A).
J Am Chem Soc. 2001 Nov 28;123(47):11678-85
Authors: Fernández CO, Cricco JA, Slutter CE, Richards JH, Gray HB, Vila AJ
Cu(A) is an electron-transfer copper center present in heme-copper oxidases and N2O reductases. The center is a binuclear unit, with...
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11-19-2010 08:44 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...
Metal-ligand interactions in perturbed blue copper sites: a paramagnetic (1)H NMR stu
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