THE TRANSITION FROM INHOMOGENEOUS TO HOMOGENEOUS KINETICS IN CO BINDING TO MYOGLOBIN

被引：37

作者：

AGMON, N

DOSTER, W

POST, F

机构：

[1] HEBREW UNIV JERUSALEM,FRITZ HABER RES CTR,IL-91904 JERUSALEM,ISRAEL

[2] TECH UNIV MUNICH,W-8046 GARCHING,GERMANY

来源：

BIOPHYSICAL JOURNAL | 1994年 / 66卷 / 05期

关键词：

D O I：

10.1016/S0006-3495(94)80953-1

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

Heme proteins react inhomogeneously with ligands at cryogenic temperatures and homogeneously at room temperature. We have identified and characterized a transition from inhomogeneous to homogeneous behavior at intermediate temperatures in the time dependence of CO binding to horse myoglobin. The turnover is attributed to a functionally important tertiary protein relaxation process during which the barrier increases dynamically. This is verified by a combination of theory and multipulse measurements. A likely biological significance of this effect is in the autocatalysis of the ligand release process.

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页码：1612 / 1622

页数：11

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