Near-Atomic Resolution Neutron Crystallography on Perdeuterated Pyrococcus furiosus Rubredoxin: Implication of Hydronium Ions and Protonation State Equilibria in Redox Changes

被引：53

作者：

Cuypers, M. G. ^{[1
,2
]}

Mason, S. A. ^{[2
]}

Blakeley, M. P. ^{[2
]}

Mitchell, E. P. ^{[1
,3
]}

Haertlein, M. ^{[2
]}

Forsyth, V. Trevor ^{[1
,2
]}

机构：

[1] Keele Univ, EPSAM ISTM, Keele ST5 5BG, Staffs, England

[2] ILL Grenoble, F-38042 Grenoble, France

[3] ESRF, Grenoble, France

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2013年 / 52卷 / 03期

基金：

英国工程与自然科学研究理事会;

关键词：

neutron crystallography; protein perdeuteration; protonation states; rubredoxin; X-ray diffraction; PROTEIN; IDENTIFICATION; DIFFRACTION; POSITIONS;

D O I：

10.1002/anie.201207071

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Neutron crystallographic analyses at near-atomic resolution are presented for both reduced and oxidized forms of perdeuterated Pyrococcus furiosus rubredoxin, a small iron-sulfur redox protein with remarkable thermostability. Hydronium ions may play a key role in the protonation and charge-transfer processes associated with the oxidized and reduced forms of the protein. Picture: overall structure showing D3O+ ions (red and gray molecules). Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

引用

页码：1022 / 1025

页数：4