引用
偶像
化学
图书馆学
计算机科学
程序设计语言
作者
T.L. Poulos,William R. Patterson,M. Sundaramoorthy
摘要
Conference Article| May 01 1995 The crystal structure of ascorbate and manganese peroxidases: the role of non-haem metal in the catalytic mechanism T. L. Poulos; T. L. Poulos 1Department of Molecular Biology & Biochemistry and Physiology & Biophysics, University of California, Irvine, CA 92717, U.S.A. Search for other works by this author on: This Site PubMed Google Scholar W. R. Patterson; W. R. Patterson 1Department of Molecular Biology & Biochemistry and Physiology & Biophysics, University of California, Irvine, CA 92717, U.S.A. Search for other works by this author on: This Site PubMed Google Scholar M. Sundaramoorthy M. Sundaramoorthy 1Department of Molecular Biology & Biochemistry and Physiology & Biophysics, University of California, Irvine, CA 92717, U.S.A. Search for other works by this author on: This Site PubMed Google Scholar Biochem Soc Trans (1995) 23 (2): 228–232. https://doi.org/10.1042/bst0230228 Article history Received: November 09 1994 Views Icon Views Article contents Figures & tables Video Audio Supplementary Data Peer Review Share Icon Share Facebook Twitter LinkedIn MailTo Cite Icon Cite Get Permissions Citation T. L. Poulos, W. R. Patterson, M. Sundaramoorthy; The crystal structure of ascorbate and manganese peroxidases: the role of non-haem metal in the catalytic mechanism. Biochem Soc Trans 1 May 1995; 23 (2): 228–232. doi: https://doi.org/10.1042/bst0230228 Download citation file: Ris (Zotero) Reference Manager EasyBib Bookends Mendeley Papers EndNote RefWorks BibTex toolbar search Search Dropdown Menu toolbar search search input Search input auto suggest filter your search All ContentAll JournalsBiochemical Society Transactions Search Advanced Search Keywords: CCP, cytochrome c peroxidase, LiP, lignin peroxidase, MnP, manganese peroxidase, APX, ascorbate peroxidase This content is only available as a PDF. © 1995 Biochemical Society1995 Article PDF first page preview Close Modal You do not currently have access to this content.
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