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.
authors.affiliation: Department of Chemistry & Institutes of Biomedical Sciences, Fudan University, Shanghai 200433, China. xstan@fudan.edu.cn.
authors.forename: Wei
authors.initials: W
authors.lastname: Li
authors.forename: Hongfei
authors.initials: H
authors.lastname: Wang
authors.forename: Zheng
authors.initials: Z
authors.lastname: Chen
authors.forename: Qing
authors.initials: Q
authors.lastname: Ye
authors.forename: Yang
authors.initials: Y
authors.lastname: Tian
authors.forename: Xin
authors.initials: X
authors.lastname: Xu
authors.forename: Zhongxian
authors.initials: Z
authors.lastname: Huang
authors.forename: Pingwei
authors.initials: P
authors.lastname: Li
authors.forename: Xiangshi
authors.initials: X
authors.lastname: Tan
mesh_terms: D016360:Clostridioides difficile / Q000201:enzymology*; D004578:Electron Spin Resonance Spectroscopy; D006801:Humans; D008670:Metals / Q000737:chemistry / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D013482:Superoxide Dismutase / Q000737:chemistry / Q000378:metabolism*
chemical_list: D008670:Metals; D013482:Superoxide Dismutase