A steric mechanism for inhibition of CO binding to heme proteins

被引：305

作者：

Kachalova, GS ^{[1
]}

Popov, AN ^{[1
]}

Bartunik, HD ^{[1
]}

机构：

[1] Max Planck Arbeitsgrp Strukturelle Mol Biol, Arbeitsgrp Prot Dynam, D-22603 Hamburg, Germany

来源：

SCIENCE | 1999年 / 284卷 / 5413期

关键词：

D O I：

10.1126/science.284.5413.473

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The crystal structures of myoglobin in the deoxy- and carbon monoxide-ligated states at a resolution of 1.15 angstroms show that carbon monoxide binding at ambient temperatures requires concerted motions of the heme, the iron, and helices E and F for relief of steric inhibition. These steps constitute the main mechanism by which heme proteins lower the affinity of the heme group for the toxic ligand carbon monoxide.

引用

页码：473 / 476

页数：4

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