Biochemical Society Transactions · 1982 · 11 citations · 0 references
Life SciencesBiochemistryMicrobiologyMetabolismMicrobial MetabolismStructural BiologyBacterial MetabolismBacterial PhysiologyElectron Transport ChainEscherichia ColiNitrate AssimilationNitrate MetabolismNitrate PathwayNitrate ReductionNitrate Respiration
Conference Article| December 01 1982 Escherichia coli formate to nitrate respiratory pathway: structural analysis DAVID BOXER; DAVID BOXER 1Department of Biochemistry, Medical Sciences Institute, University of Dundee, Dundee DD1 4HN, U.K. Search for other works by this author on: This Site PubMed Google Scholar AILSA MALCOLM; AILSA MALCOLM 2Department of Biochemistry, Medical Sciences Institute, University of Dundee, Dundee DD1 4HN, U.K. Search for other works by this author on: This Site PubMed Google Scholar ALEXANDER GRAHAM ALEXANDER GRAHAM * 3Department of Biochemistry, Medical Sciences Institute, University of Dundee, Dundee DD1 4HN, U.K. Search for other works by this author on: This Site PubMed Google Scholar Biochem Soc Trans (1982) 10 (6): 480–481. https://doi.org/10.1042/bst0100480 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 DAVID BOXER, AILSA MALCOLM, ALEXANDER GRAHAM; Escherichia coli formate to nitrate respiratory pathway: structural analysis. Biochem Soc Trans 1 December 1982; 10 (6): 480–481. doi: https://doi.org/10.1042/bst0100480 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: DDISA, diazotized di-iodosulphanilic acid, DABS, diazobenzenesulphonate This content is only available as a PDF. © 1982 Biochemical Society1982 Article PDF first page preview Close Modal You do not currently have access to this content.