Related ArticlesElectronic 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 redox potential in its class, has been investigated through (1)H nuclear magnetic resonance applied to its cobalt(II) derivative. The assignment of the protons belonging to the coordinated residues has been performed. Many other amino acids situated in the vicinity of the metal ion, including six hydrophobic residues (isoleucine140 and five phenylalanines) have also been identified. The orientation of the main axes of the magnetic susceptibility tensor for the cobalt(II)-rusticyanin as well as its axial, Deltachi(ax), and rhombic, Deltachi(rh), magnetic susceptibility anisotropy components have been determined. A comparison of the present results with those previously obtained for cobalt(II)azurin [Donaire, A., Salgado, J., Moratal, J. M. (1998) Biochemistry 37, 8659-8673] allows us to provide further insights into the reasons for the high redox potential of this protein. According to our results, the interaction between the metal ion and the thioether Sdelta of the axial methionine is not as influential as the strong destabilizing effect that the hydrophobic residues close to the metal ion undergo in the oxidized state.
[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...
nmrlearner
Journal club
0
11-24-2010 09:01 PM
[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...
nmrlearner
Journal club
0
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...
nmrlearner
Journal club
0
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...
nmrlearner
Journal club
0
11-24-2010 08:49 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...
nmrlearner
Journal club
0
11-19-2010 08:44 PM
NMR Characterization of Copper-Binding Domains 4-6 of ATP7B,
NMR Characterization of Copper-Binding Domains 4-6 of ATP7B,
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi1008535/aop/images/medium/bi-2010-008535_0002.gif
Biochemistry
DOI: 10.1021/bi1008535
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/5w8PZPbbOyQ
More...
nmrlearner
Journal club
0
09-11-2010 01:25 AM
Comprehensive Solid-State NMR Characterization of Electronic Structure in Ditechnetiu
Comprehensive Solid-State NMR Characterization of Electronic Structure in Ditechnetium Heptoxide
Herman Cho et al
http://pubs.acs.org//appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja105687j/aop/images/medium/ja-2010-05687j_0002.gifJournal of the American Chemical Society, Volume 0, Issue 0, Articles ASAP (As Soon As Publishable).
Source: Journal of the American Chemical Society
nmrlearner
Journal club
0
09-01-2010 10:56 AM
[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...