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Rational design of a mononuclear metal site into the archaeal Rieske-type protein scaffold
Iwasaki, T; Kounosu, A; Tao Y(陶冶); Tao, Y; Li, ZR; Shokes, JE; Cosper, NJ; Imai, T; Urushiyama, A; Scott, RA
2005
Source PublicationJOURNAL OF BIOLOGICAL CHEMISTRY
Volume280Issue:10Pages:9129-9134
Corresponding AuthorNippon Med Coll, Dept Biochem & Mol Biol, Bunkyo Ku, Tokyo 1138602, Japan ; Nippon Med Coll, Dept Biochem & Mol Biol, Bunkyo Ku, Tokyo 1138602, Japan ; Chinese Acad Sci, Synchrotron Radiat Facil, Inst High Energy Phys, Beijing 100039, Peoples R China ; Rikkyo Univ, Dept Chem, Toshima Ku, Tokyo 1718501, Japan ; Univ Georgia, Dept Chem, Athens, GA 30602 USA
SubtypeArticle
AbstractProteins containing Rieske-type [2Fe-2S] clusters play essential functions in all three domains of life. We engineered the two histidine ligands to the Rieske-type [2Fe2S] cluster in the hyperthermophilic archaeal Rieske-type ferredoxin from Sulfolobus solfataricus to modify types and spacing of ligands and successfully converted the metal and cluster type at the redox-active site with a minimal structural change to a native Rieske-type protein scaffold. Spectroscopic analyses unambiguously established a rubredoxin-type mononuclear Fe3+/2+ center at the engineered local metal-binding site ( Zn2+ occupies the iron site depending on the expression conditions). These results show the importance of types and spacing of ligands in the in vivo cluster recognition/ insertion/ assembly in biological metallosulfur protein scaffolds. We suggest that early ligand substitution and displacement events at the local metal-binding site(s) might have primarily allowed the metal and cluster type conversion in ancestral redox protein modules, which greatly enhanced their capabilities of conducting a wide range of unique redox chemistry in biological electron transfer conduits, using a limited number of basic protein scaffolds.
Subject AreaBiochemistry & Molecular Biology
DOI10.1074/jbc.M414051200
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Indexed ByINSPIREHEP
Language英语
WOS Research AreaBiochemistry & Molecular Biology
WOS SubjectBiochemistry & Molecular Biology
WOS IDWOS:000227453100062
inspireid684733
inspireURLhttps://inspirehep.net/literature/684733
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Document Type期刊论文
Identifierhttp://ir.ihep.ac.cn/handle/311005/240157
Collection多学科研究中心
Affiliation中国科学院高能物理研究所
First Author AffilicationInstitute of High Energy
Recommended Citation
GB/T 7714
Iwasaki, T,Kounosu, A,Tao Y,et al. Rational design of a mononuclear metal site into the archaeal Rieske-type protein scaffold[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2005,280(10):9129-9134.
APA Iwasaki, T.,Kounosu, A.,陶冶.,Tao, Y.,Li, ZR.,...&Scott, RA.(2005).Rational design of a mononuclear metal site into the archaeal Rieske-type protein scaffold.JOURNAL OF BIOLOGICAL CHEMISTRY,280(10),9129-9134.
MLA Iwasaki, T,et al."Rational design of a mononuclear metal site into the archaeal Rieske-type protein scaffold".JOURNAL OF BIOLOGICAL CHEMISTRY 280.10(2005):9129-9134.
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