Probing the metal specificity mechanism of superoxide dismutase from human pathogen clostridium difficile

Wei Li; Hongfei Wang; Zheng Chen; Qing Ye; Yang Tian; Xin Xu; Zhongxian Huang; Pingwei Li; Xiangshi Tan

doi:10.1039/c3cc47859a

Probing the metal specificity mechanism of superoxide dismutase from human pathogen clostridium difficile

Wei Li
, Hongfei Wang
, Zheng Chen
, Qing Ye
, Yang Tian
, Xin Xu
, Zhongxian Huang
, Pingwei Li
, Xiangshi Tan^*

^*此作品的通讯作者

科研成果: 期刊稿件 › 文章 › 同行评审

7 引用（Scopus）

摘要

The molecular mechanism of the metal specificity to superoxide dismutase from human pathogen C. difficile (SOD_cd) was investigated by X-ray crystallography, spectroscopy, SOD activity assay, electrochemistry, and DFT calculations, and the results indicate that the cognate metal characters tuned by the metal micro-environment dominate the metal specificity of the SOD_cd.

源语言	英语
页（从-至）	584-586
页数	3
期刊	Chemical Communications
卷	50
期	5
DOI	https://doi.org/10.1039/c3cc47859a
出版状态	已出版 - 10 12月 2014
已对外发布	是

访问文件

10.1039/c3cc47859a

其它文件与链接

链接到 Scopus 的出版物

引用此

@article{f60dec7e2930460c8109582a5a0ce1b3,

title = "Probing the metal specificity mechanism of superoxide dismutase from human pathogen clostridium difficile",

abstract = "The molecular mechanism of the metal specificity to superoxide dismutase from human pathogen C. difficile (SODcd) was investigated by X-ray crystallography, spectroscopy, SOD activity assay, electrochemistry, and DFT calculations, and the results indicate that the cognate metal characters tuned by the metal micro-environment dominate the metal specificity of the SODcd.",

author = "Wei Li and Hongfei Wang and Zheng Chen and Qing Ye and Yang Tian and Xin Xu and Zhongxian Huang and Pingwei Li and Xiangshi Tan",

year = "2014",

month = dec,

day = "10",

doi = "10.1039/c3cc47859a",

language = "英语",

volume = "50",

pages = "584--586",

journal = "Chemical Communications",

issn = "1359-7345",

publisher = "Royal Society of Chemistry",

number = "5",

}

TY - JOUR

T1 - Probing the metal specificity mechanism of superoxide dismutase from human pathogen clostridium difficile

AU - Li, Wei

AU - Wang, Hongfei

AU - Chen, Zheng

AU - Ye, Qing

AU - Tian, Yang

AU - Xu, Xin

AU - Huang, Zhongxian

AU - Li, Pingwei

AU - Tan, Xiangshi

PY - 2014/12/10

Y1 - 2014/12/10

N2 - The molecular mechanism of the metal specificity to superoxide dismutase from human pathogen C. difficile (SODcd) was investigated by X-ray crystallography, spectroscopy, SOD activity assay, electrochemistry, and DFT calculations, and the results indicate that the cognate metal characters tuned by the metal micro-environment dominate the metal specificity of the SODcd.

AB - The molecular mechanism of the metal specificity to superoxide dismutase from human pathogen C. difficile (SODcd) was investigated by X-ray crystallography, spectroscopy, SOD activity assay, electrochemistry, and DFT calculations, and the results indicate that the cognate metal characters tuned by the metal micro-environment dominate the metal specificity of the SODcd.

UR - https://www.scopus.com/pages/publications/84890330753

U2 - 10.1039/c3cc47859a

DO - 10.1039/c3cc47859a

M3 - 文章

C2 - 24275896

AN - SCOPUS:84890330753

SN - 1359-7345

VL - 50

SP - 584

EP - 586

JO - Chemical Communications

JF - Chemical Communications

IS - 5

ER -

Probing the metal specificity mechanism of superoxide dismutase from human pathogen clostridium difficile

摘要

访问文件

其它文件与链接

指纹

引用此