Comparison of ligand migration and binding in heme proteins of the globin family

作     者：Karin Nienhaus G.Ulrich Nienhaus 

作者机构：Institute of Applied Physics (APH) Karlsruhe Institute of Technology (KIT) Institute of Nanotechnology (INT) and Institute of Toxicology and Genetics (ITG) Karlsruhe Institute of Technology (KIT) Department of Physics University of Illinois at Urbana-Champaign 

出 版 物：《Chinese Physics B》 (中国物理B（英文版）)

年 卷 期：2015年第24卷第12期

页      面：109-118页

核心收录：

学科分类：0710[理学-生物学] 071010[理学-生物化学与分子生物学] 081704[工学-应用化学] 07[理学] 08[工学] 0817[工学-化学工程与技术] 0702[理学-物理学] 

基　　金：supported by the Deutsche Forschungsgemeinschaft (DFG  grant Ni291/10) 

主　　题：flash photolysis ligand binding time-resolved spectroscopy heme protein 

摘      要：The binding of small diatomic ligands such as carbon monoxide or dioxygen to heme proteins is among the simplest biological processes known. Still, it has taken many decades to understand the mechanistic aspects of this process in full detail. Here, we compare ligand binding in three heme proteins of the globin family, myoglobin, a dimeric hemoglobin, and neuroglobin. The combination of structural, spectroscopic, and kinetic experiments over many years by many laboratories has revealed common properties of globins and a clear mechanistic picture of ligand binding at the molecular level. In addition to the ligand binding site at the heme iron, a primary ligand docking site exists that ensures efficient ligand binding to and release from the heme iron. Additional, secondary docking sites can greatly facilitate ligand escape after its dissociation from the heme. Although there is only indirect evidence at present, a preformed histidine gate appears to exist that allows ligand entry to and exit from the active site. The importance of these features can be assessed by studies involving modified proteins（via site-directed mutagenesis） and comparison with heme proteins not belonging to the globin family.