RELAXATION DYNAMICS OF MYOGLOBIN IN SOLUTION

被引:125
作者
TIAN, WD
SAGE, JT
SRAJER, V
CHAMPION, PM
机构
[1] Department of Physics, Northeastern University, Boston
关键词
D O I
10.1103/PhysRevLett.68.408
中图分类号
O4 [物理学];
学科分类号
0702 ;
摘要
The geminate rebinding kinetics of MbCO in solution at high temperature (260-300 K) shows nonexponential behavior (stretched, beta approximately 1/2) that may be related to nonequilibrium relaxation of the distal pocket. A two-pulse photolysis experiment, which probes a kinetically selected subpopulation, demonstrates that the nonexponential behavior arises from a fluctuationally averaged system and also reveals slow interconversion times for large-scale protein motions. Measurements as a function of temperature lead to a direct determination of the Arrhenius barrier at the heme (18 +/- 2 kJ/mole).
引用
收藏
页码:408 / 411
页数:4
相关论文
共 23 条
[21]   INVESTIGATION OF LASER-INDUCED LONG-LIVED STATES OF PHOTOLYZED MBCO [J].
SRAJER, V ;
REINISCH, L ;
CHAMPION, PM .
BIOCHEMISTRY, 1991, 30 (20) :4886-4895
[22]   LIGAND-BINDING TO HEME-PROTEINS - CONNECTION BETWEEN DYNAMICS AND FUNCTION [J].
STEINBACH, PJ ;
ANSARI, A ;
BERENDZEN, J ;
BRAUNSTEIN, D ;
CHU, K ;
COWEN, BR ;
EHRENSTEIN, D ;
FRAUENFELDER, H ;
JOHNSON, JB ;
LAMB, DC ;
LUCK, S ;
MOURANT, JR ;
NIENHAUS, GU ;
ORMOS, P ;
PHILIPP, R ;
XIE, AH ;
YOUNG, RD .
BIOCHEMISTRY, 1991, 30 (16) :3988-4001
[23]  
ZHU L, IN PRESS J MOL BIOL