title: Low stability of the reduced state of Mycobacterium tuberculosis NrdH redoxin.
abstract: NrdH redoxin is the only hydrogen donor for ribonucleotide reductase in Mycobacterium tuberculosis. Several crystal structures of NrdH redoxins in the oxidized state from different species have been reported, but no structure of the reduced state has yet been reported. Using NMR spectroscopy, we found surprisingly that the reduced NrdH redoxin from M. tuberculosis is largely unfolded at a pH lower than the pKa of its first active site cysteine, and the structural basis of the low stability was analyzed. In addition, a single mutant of the NrdH redoxin suitable to determine the structure in the reduced state was obtained.
authors.affiliation: Shandong Key Laboratory of Synthetic Biology, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, China.|Qingdao Engineering Laboratory of Single Cell Oil, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, China.|CAS Key Laboratory of Biofuels, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, China.
authors.forename: Ya-Jun
authors.initials: YJ
authors.lastname: Liu
authors.affiliation: Department of Biological Science and Engineering, School of Chemical and Biological Engineering, University of Science and Technology Beijing, China.
authors.forename: Xiaxia
authors.initials: X
authors.lastname: Song
authors.affiliation: Shandong Key Laboratory of Synthetic Biology, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, China.|Qingdao Engineering Laboratory of Single Cell Oil, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, China.|CAS Key Laboratory of Biofuels, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, China.
authors.forename: Yifei
authors.initials: Y
authors.lastname: Li
authors.affiliation: Department of Biological Science and Engineering, School of Chemical and Biological Engineering, University of Science and Technology Beijing, China.
authors.forename: Jinsong
authors.initials: J
authors.lastname: Xuan
authors.affiliation: Shandong Key Laboratory of Synthetic Biology, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, China.|Qingdao Engineering Laboratory of Single Cell Oil, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, China.|CAS Key Laboratory of Biofuels, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, China.
authors.forename: Qiu
authors.initials: Q
authors.lastname: Cui
authors.affiliation: National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.
authors.forename: Jinfeng
authors.initials: J
authors.lastname: Wang
authors.affiliation: Shandong Key Laboratory of Synthetic Biology, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, China.|Qingdao Engineering Laboratory of Single Cell Oil, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, China.|CAS Key Laboratory of Biofuels, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, China.
authors.forename: Yingang
authors.initials: Y
authors.lastname: Feng
mesh_terms: D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D020134:Catalytic Domain; D048230:Corynebacterium glutamicum / Q000378:metabolism; D003545:Cysteine / Q000737:chemistry; D004926:Escherichia coli / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D050505:Mutant Proteins / Q000737:chemistry / Q000378:metabolism; D009169:Mycobacterium tuberculosis / Q000378:metabolism*; D019906:Nuclear Magnetic Resonance, Biomolecular; D010084:Oxidation-Reduction; D055550:Protein Stability; D058767:Protein Unfolding; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D016415:Sequence Alignment; D013879:Thioredoxins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D050505:Mutant Proteins; C107179:NrdH protein, E Coli; D011994:Recombinant Proteins; D013879:Thioredoxins; D003545:Cysteine
keywords: Mycobacterium tuberculosis; NMR; NrdH redoxin; protein stability; protein structure