このエントリーをはてなブックマークに追加
ID 53953
FullText URL
Author
Tsunekawa, Naoki
Hirano, Toshiyuki
Sato, Fumitoshi
Abstract
Oxygen tolerance of selenium-containing [NiFeSe] hydrogenases (Hases) is attributable to the high reducing power of the selenocysteine residue, which sustains the bimetallic Ni–Fe catalytic center in the large subunit. Genes encoding [NiFeSe] Hases are inherited by few sulphate-reducing δ-proteobacteria globally distributed under various anoxic conditions. Ancestral sequences of [NiFeSe] Hases were elucidated and their three-dimensional structures were recreated in silico using homology modelling and molecular dynamic simulation, which suggested that deep gas channels gradually developed in [NiFeSe] Hases under absolute anaerobic conditions, whereas the enzyme remained as a sealed edifice under environmental conditions of a higher oxygen exposure risk. The development of a gas cavity appears to be driven by non-synonymous mutations, which cause subtle conformational changes locally and distantly, even including highly conserved sequence regions.
Note
This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
Published Date
2016-01-28
Publication Title
Scientific reports
Volume
volume6
Publisher
Nature Publishing Group
Start Page
19742
ISSN
2045-2322
Content Type
Journal Article
Official Url
http://dx.doi.org/10.1038/srep19742
language
英語
Copyright Holders
© 2016 Nature Publishing Group
File Version
publisher
Refereed
True
DOI
PubMed ID
Web of Sience KeyUT