Thermodynamic analysis of hydration in human serum heme-albumin

被引:6
作者
Baroni, Simona [3 ]
Pariani, Giorgio [1 ,2 ]
Fanali, Gabriella [1 ,2 ]
Longo, Dario [4 ,5 ]
Ascenzi, Paolo [6 ,7 ]
Aime, Silvio [4 ,5 ]
Fasano, Mauro [1 ,2 ]
机构
[1] Univ Insubria, Dept Struct & Funct Biol, I-21052 Busto Arsizio, VA, Italy
[2] Univ Insubria, Ctr Neurosci, I-21052 Busto Arsizio, VA, Italy
[3] Univ Turin, Invento Srl Co Incubator, I-10126 Turin, Italy
[4] Univ Turin, Dept Chem IFM, I-10126 Turin, Italy
[5] Univ Turin, Ctr Mol Imaging CIM, I-10126 Turin, Italy
[6] Univ Roma Tre, Dept Biol, I-00146 Rome, Italy
[7] Univ Roma Tre, Interdept Lab Electron Microscopy, I-00146 Rome, Italy
关键词
Human serum albumin; Ferric human serum heme-albumin; Heme-protein hydration; NMR relaxation; MAGNETIC-RELAXATION DISPERSION; MODEL-FREE ANALYSIS; ACID-BINDING SITES; H-1 NMRD PROFILES; ALLOSTERIC MODULATION; HUMAN HEMALBUMIN; LIGAND-BINDING; IRON GEOMETRY; DRUG-BINDING; MYOGLOBIN;
D O I
10.1016/j.bbrc.2009.05.075
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Ferric human serum heme-albumin (heme-HSA) shows a peculiar nuclear magnetic relaxation dispersion (NMRD) behavior that allows to investigate structural and functional properties. Here, we report a thermodynamic analysis of NMRD profiles of heme-HSA between 20 and 60 degrees C to characterize its hydration. NMRD profiles, all showing two Lorentzian dispersions at 0.3 and 60 MHz, were analyzed in terms of modulation of the zero field splitting tensor for the S = 5/2 manifold. Values of correlation times for tensor fluctuation (tau(nu)) and chemical exchange of water molecules (tau(M)) show the expected temperature dependence, with activation enthalpies of -1.94 and -2.46 +/- 0.2 kJ mol (1), respectively. The cluster of water molecules located in the close proximity of the heme is progressively reduced in size by increasing the temperature, with Delta H = 68 +/- 28 kJ mol(-1) and Delta S = 200 +/- 80 J mol (1) K (1). These results highlight the role of the water solvent in heme-HSA structure-function relationships. (C) 2009 Elsevier Inc. All riglits reserved.
引用
收藏
页码:385 / 389
页数:5
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