Related Articles1H-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, Jim矇nez HR, Donaire A, Moratal JM
Substitution of copper by cobalt in blue copper proteins gives a paramagnetic metalloderivative suitable for paramagnetic NMR studies. A thorough analysis of the 1H-NMR spectrum of Pseudomonas aeruginosa Co(II)-azurin is presented here. All the observable contact-shifted signals as well as many other paramagnetic signals from protons placed up to about 1.0 nm around the metal center, including some residues belonging to functionally important parts of the protein like the hydrophobic patch and the His35 region, have been assigned. The results obtained permit the detection and study of structural variations like those originated by the His35 ionization, and allow us to draw a feasible picture of the metal coordination site. Contact-shifted signals correspond to the same five residues which are found in the coordination sphere of the native Cu(II)-azurin, i.e. His46, His117, Cys112, Met121 and Gly45. Among them, the histidine residues present a pattern of resonances typical for histidines coordinated to cobalt in other cobalt protein derivatives, and the cysteine signals clearly indicate a strong interaction with the paramagnetic Co(II) ion. In contrast, the Met121 signals indicate a weak but still existent contact interaction with the metal center. On the other hand, the very weak copper ligand, Gly45, appears here as clearly coordinated to cobalt. Results are consistent with a distorted tetrahedral metal site with the cobalt deviated from the N2S plane towards the Gly45 O axial position and weakly interacting with the Met121 sulfur.
Metabolic relationship between polyhydroxyalkanoic acid and rhamnolipid synthesis in Pseudomonas aeruginosa: comparative 像C NMR analysis of the products in wild-type and mutants.
Metabolic relationship between polyhydroxyalkanoic acid and rhamnolipid synthesis in Pseudomonas aeruginosa: comparative 像C NMR analysis of the products in wild-type and mutants.
Metabolic relationship between polyhydroxyalkanoic acid and rhamnolipid synthesis in Pseudomonas aeruginosa: comparative 像C NMR analysis of the products in wild-type and mutants.
J Biotechnol. 2011 Jan 10;151(1):30-42
Authors: Choi MH, Xu J, Gutierrez M, Yoo T, Cho YH, Yoon SC
Polyhydroxyalkanoic acids (PHAs) and rhamnolipids considered as biotechnologically important...
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Targeting Bacterial Membranes: Identification of Pseudomonas aeruginosa D-Arabinose-5P Isomerase and NMR Characterisation of its Substrate Recognition and Binding Properties.
Targeting Bacterial Membranes: Identification of Pseudomonas aeruginosa D-Arabinose-5P Isomerase and NMR Characterisation of its Substrate Recognition and Binding Properties.
Targeting Bacterial Membranes: Identification of Pseudomonas aeruginosa D-Arabinose-5P Isomerase and NMR Characterisation of its Substrate Recognition and Binding Properties.
Chembiochem. 2011 Feb 17;
Authors: Airoldi C, Sommaruga S, Merlo S, Sperandeo P, Cipolla L, Polissi A, Nicotra F
The identification and characterisation of Pseudomonas aeruginosa KdsD (Pa-KdsD), a...
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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] 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] 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, Jim幯ez B, Moratal J, Hall JF, Hasnain SS
The oxidized state of rusticyanin, the blue copper protein with the highest...
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[NMR paper] Paramagnetic NMR Spectroscopy of Cobalt(II) and Copper(II) Derivatives of Pseudomonas
Paramagnetic NMR Spectroscopy of Cobalt(II) and Copper(II) Derivatives of Pseudomonas aeruginosa His46Asp Azurin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Paramagnetic NMR Spectroscopy of Cobalt(II) and Copper(II) Derivatives of Pseudomonas aeruginosa His46Asp Azurin.
Inorg Chem. 1997 Sep 24;36(20):4567-4570
Authors: Vila AJ, Ramirez BE, Di Bilio AJ, Mizoguchi TJ, Richards JH, Gray HB
NMR spectra of paramagnetic Co(II) and Cu(II) derivatives of Pseudomonas aeruginosa His46Asp...
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[NMR paper] Solution structure of Fe(II) cytochrome c551 from Pseudomonas aeruginosa as determine
Solution structure of Fe(II) cytochrome c551 from Pseudomonas aeruginosa as determined by two-dimensional 1H NMR.
Related Articles Solution structure of Fe(II) cytochrome c551 from Pseudomonas aeruginosa as determined by two-dimensional 1H NMR.
Biochemistry. 1991 Sep 17;30(37):9040-6
Authors: Detlefsen DJ, Thanabal V, Pecoraro VL, Wagner G
The solution structure of Fe(II) cytochrome c551 from Pseudomonas aeruginosa based on 2D 1H NMR data is reported. Two sets of structure calculations were completed with a combination of simulated annealing...
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[NMR paper] Solution structure of Fe(II) cytochrome c551 from Pseudomonas aeruginosa as determine
Solution structure of Fe(II) cytochrome c551 from Pseudomonas aeruginosa as determined by two-dimensional 1H NMR.
Related Articles Solution structure of Fe(II) cytochrome c551 from Pseudomonas aeruginosa as determined by two-dimensional 1H NMR.
Biochemistry. 1991 Sep 17;30(37):9040-6
Authors: Detlefsen DJ, Thanabal V, Pecoraro VL, Wagner G
The solution structure of Fe(II) cytochrome c551 from Pseudomonas aeruginosa based on 2D 1H NMR data is reported. Two sets of structure calculations were completed with a combination of simulated annealing...