Heme-solvent coupling: A Mossbauer study of myoglobin in sucrose

被引:75
作者
Lichtenegger, H
Doster, W
Kleinert, T
Birk, A
Sepiol, B
Vogl, G
机构
[1] Univ Vienna, Inst Mat Phys, A-1090 Vienna, Austria
[2] Tech Univ Munich, Fak Phys E13 17, D-85747 Garching, Germany
关键词
D O I
10.1016/S0006-3495(99)77208-5
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
The Mossbauer effect of Fe-57-enriched samples was used to investigate the coupling of 80% sucrose/water, a protein-stabilizing solvent, to vibrational and diffusive modes of the heme iron of CO-myoglobin. For comparison we also determined the Mossbauer spectra of (K4Fe)-Fe-57 (CN)(6) (potassium ferrocyanide, PFC), where the iron is fully exposed in the same solvent. The temperature dependence of the Mossbauer parameters derived for the two samples proved to be remarkably similar, indicative of a strong coupling of the main heme displacements to the viscoelastic relaxation of the solvent. We show that CO escape out of the heme pocket couples to the same type of fluctuations, whereas intramolecular bond formation involves solvent-decoupled heme deformation modes that are less prominent in the Mossbauer spectrum. With respect to other solvents, however, sucrose shows a reduced viscosity effect on heme displacements and the kinetics of ligand binding due to preferential hydration of the protein. This result confirms thermodynamic predictions of the stabilizing action of sucrose by a dynamic method.
引用
收藏
页码:414 / 422
页数:9
相关论文
共 49 条
[1]   CONFORMATIONAL RELAXATION AND LIGAND-BINDING IN MYOGLOBIN [J].
ANSARI, A ;
JONES, CM ;
HENRY, ER ;
HOFRICHTER, J ;
EATON, WA .
BIOCHEMISTRY, 1994, 33 (17) :5128-5145
[2]   THE ROLE OF SOLVENT VISCOSITY IN THE DYNAMICS OF PROTEIN CONFORMATIONAL-CHANGES [J].
ANSARI, A ;
JONES, CM ;
HENRY, ER ;
HOFRICHTER, J ;
EATON, WA .
SCIENCE, 1992, 256 (5065) :1796-1798
[3]   DYNAMICS OF LIGAND-BINDING TO MYOGLOBIN [J].
AUSTIN, RH ;
BEESON, KW ;
EISENSTEIN, L ;
FRAUENFELDER, H ;
GUNSALUS, IC .
BIOCHEMISTRY, 1975, 14 (24) :5355-5373
[4]   SOLVENT VISCOSITY AND PROTEIN DYNAMICS [J].
BEECE, D ;
EISENSTEIN, L ;
FRAUENFELDER, H ;
GOOD, D ;
MARDEN, MC ;
REINISCH, L ;
REYNOLDS, AH ;
SORENSEN, LB ;
YUE, KT .
BIOCHEMISTRY, 1980, 19 (23) :5147-5157
[5]   MODES OF STABILIZATION OF A PROTEIN BY ORGANIC SOLUTES DURING DESICCATION [J].
CARPENTER, JF ;
CROWE, JH .
CRYOBIOLOGY, 1988, 25 (05) :459-470
[6]   THE MECHANISM OF CRYOPROTECTION OF PROTEINS BY SOLUTES [J].
CARPENTER, JF ;
CROWE, JH .
CRYOBIOLOGY, 1988, 25 (03) :244-255
[7]   AN INFRARED SPECTROSCOPIC STUDY OF THE INTERACTIONS OF CARBOHYDRATES WITH DRIED PROTEINS [J].
CARPENTER, JF ;
CROWE, JH .
BIOCHEMISTRY, 1989, 28 (09) :3916-3922
[8]   Is trehalose special for preserving dry biomaterials? [J].
Crowe, LM ;
Reid, DS ;
Crowe, JH .
BIOPHYSICAL JOURNAL, 1996, 71 (04) :2087-2093
[9]   Vibrational frequency shifts as a probe of hydrogen bonds: thermal expansion and glass transition of myoglobin in mixed solvents [J].
Demmel, F ;
Doster, W ;
Petry, W ;
Schulte, A .
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS, 1997, 26 (04) :327-335
[10]   Water-coupled low-frequency modes of myoglobin and lysozyme observed by inelastic neutron scattering [J].
Diehl, M ;
Doster, W ;
Petry, W ;
Schober, H .
BIOPHYSICAL JOURNAL, 1997, 73 (05) :2726-2732