Backbone Dynamics of Rusticyanin: The High Hydrophobicity and Rigidity of This Blue Copper Protein Is Responsible for Its Thermodynamic Properties†
作者： Beatriz Jiménez , Mario Piccioli , José-María Moratal , Antonio Donaire
DOI: 10.1021/BI034692Q
关键词: Metal 、 Protein structure 、 Amide 、 Solvent 、 Heteronuclear molecule 、 Chemistry 、 Copper protein 、 Crystallography 、 Rusticyanin 、 Nuclear magnetic resonance spectroscopy 、 Biochemistry
摘要: Local dynamics and solute-solvent exchange properties of rusticyanin (Rc) from Thiobacillus ferrooxidans have been studied by applying heteronuclear ((1)H, (15)N) NMR spectroscopy. (15)N relaxation parameters determined for the reduced protein, a model-free analysis has applied. The high average value generalized order parameter, S(2) (0.93), indicates that Rc is very rigid. cross correlation rates recorded in both oxidized forms conclusively proves possesses same dynamic features oxidation states. accessibility backbone amide protons to solvent at different time scales also specific pulse sequences H(2)O/D(2)O experiments. These experiments reveal extremely hydrophobic. first N-35 amino acids, not present other BCPs, protect beta-barrel core its interaction with solvent, thus, this one main factors contributing hydrophobicity. Both characteristics (high rigidity hydrophobicity) are maintained metal ion surroundings.
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sci-hub.se 参考文章(24)
R.M. Brunne, E. Liepinsh, G. Otting, K. Wüthrich, W.F. van Gunsteren, Hydration of proteins. A comparison of experimental residence times of water molecules solvating the bovine pancreatic trypsin inhibitor with theoretical model calculations Journal of Molecular Biology. ,vol. 231, pp. 1040- 1048 ,(1993) , 10.1006/JMBI.1993.1350
Sophie Zinn-Justin, Patrick Berthault, Marc Guenneugues, Hervé Desvaux, Off-resonance rf fields in heteronuclear NMR: Application to the study of slow motions Journal of Biomolecular NMR. ,vol. 10, pp. 363- 372 ,(1997) , 10.1023/A:1018365815186
Paul D. Barker, Ivano Bertini, Rebecca Del Conte, Stuart J. Ferguson, Parvana Hajieva, Esther Tomlinson, Paola Turano, Maria Silvia Viezzoli, A further clue to understanding the mobility of mitochondrial yeast cytochrome c FEBS Journal. ,vol. 268, pp. 4468- 4476 ,(2001) , 10.1046/J.1432-1327.2001.02369.X
Ivano Bertini, J.Gaspard Huber, Claudio Luchinat, Mario Piccioli, Protein hydration and location of water molecules in oxidized horse heart cytochrome c by (1)H NMR. Journal of Magnetic Resonance. ,vol. 147, pp. 1- 8 ,(2000) , 10.1006/JMRE.2000.2131
C.M. Groeneveld, M.C. Ouwerling, C. Erkelens, G.W. Canters, 1H nuclear magnetic resonance study of the protonation behaviour of the histidine residues and the electron self-exchange reaction of azurin from Alcaligenes denitrificans. Journal of Molecular Biology. ,vol. 200, pp. 189- 199 ,(1988) , 10.1016/0022-2836(88)90343-9
Antonio Donaire, Beatriz Jiménez, Claudio O. Fernández, Roberta Pierattelli, Tomotake Niizeki, José-María Moratal, John F. Hall, Takamitsu Kohzuma, S. Samar Hasnain, Alejandro J. Vila, Metal-ligand interplay in blue copper proteins studied by 1H NMR spectroscopy: Cu(II)-pseudoazurin and Cu(II)-rusticyanin. Journal of the American Chemical Society. ,vol. 124, pp. 13698- 13708 ,(2002) , 10.1021/JA0267019
D. W. Randall, D. R. Gamelin, L. B. LaCroix, E. I. Solomon, Electronic structure contributions to electron transfer in blue Cu and CuA JBIC Journal of Biological Inorganic Chemistry. ,vol. 5, pp. 16- 29 ,(2000) , 10.1007/S007750050003
Azita Mesgarzadeh, Stefania Pfeiffer, Jan Engelke, Dirck Lassen, Heinz Ruterjans, Bound water in apo and holo bovine heart fatty-acid-binding protein determined by heteronuclear NMR spectroscopy FEBS Journal. ,vol. 251, pp. 781- 786 ,(1998) , 10.1046/J.1432-1327.1998.2510781.X
Claudio Dalvit, Ulrich Hommel, Sensitivity-Improved Detection of Protein Hydration and Its Extension to the Assignment of Fast-Exchanging Resonances Journal of Magnetic Resonance, Series B. ,vol. 109, pp. 334- 338 ,(1995) , 10.1006/JMRB.1995.9984
Lalji D Kanbi, Svetlana Antonyuk, Michael A Hough, John F Hall, Fraser E Dodd, S Samar Hasnain, None, Crystal structures of the Met148Leu and Ser86Asp mutants of rusticyanin from Thiobacillus ferrooxidans: insights into the structural relationship with the cupredoxins and the multi copper proteins. Journal of Molecular Biology. ,vol. 320, pp. 263- 275 ,(2002) , 10.1016/S0022-2836(02)00443-6