Unanticipated coordination of tris buffer to the Radical SAM cluster of the RimO methylthiotransferase.

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  • Additional Information
    • Source:
      Publisher: Springer Country of Publication: Germany NLM ID: 9616326 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1432-1327 (Electronic) Linking ISSN: 09498257 NLM ISO Abbreviation: J Biol Inorg Chem Subsets: MEDLINE
    • Publication Information:
      Original Publication: Berlin : Springer, c1996-
    • Subject Terms:
      S-Adenosylmethionine/*chemistry ; Sulfurtransferases/*chemistry ; Tromethamine/*chemistry; Buffers ; S-Adenosylmethionine/metabolism ; Sulfurtransferases/metabolism ; Thermotoga maritima/enzymology
    • Abstract:
      Radical SAM enzymes generally contain a [4Fe-4S](2+/1+) (RS cluster) cluster bound to the protein via the three cysteines of a canonical motif CxxxCxxC. The non-cysteinyl iron is used to coordinate SAM via its amino-carboxylate moiety. The coordination-induced proximity between the cluster acting as an electron donor and the adenosyl-sulfonium bond of SAM allows for the homolytic cleavage of the latter leading to the formation of the reactive 5'-deoxyadenosyl radical used for substrate activation. Most of the structures of Radical SAM enzymes have been obtained in the presence of SAM, and therefore, little is known about the situation when SAM is not present. In this report, we show that RimO, a methylthiotransferase belonging to the radical SAM superfamily, binds a Tris molecule in the absence of SAM leading to specific spectroscopic signatures both in Mössbauer and pulsed EPR spectroscopies. These data provide a cautionary note for researchers who work with coordinative unsaturated iron sulfur clusters.
    • References:
      Nat Chem Biol. 2013 May;9(5):333-8. (PMID: 23542644)
      Methods Enzymol. 1988;158:357-64. (PMID: 3374387)
      Proc Natl Acad Sci U S A. 2008 Feb 12;105(6):1826-31. (PMID: 18252828)
      J Am Chem Soc. 2005 Jul 6;127(26):9612-24. (PMID: 15984889)
      J Am Chem Soc. 2013 Oct 16;135(41):15404-15416. (PMID: 23991893)
      Anal Biochem. 1983 Jun;131(2):373-8. (PMID: 6614472)
      Science. 1997 Aug 1;277(5326):653-9. (PMID: 9235882)
      J Am Chem Soc. 2009 Sep 23;131(37):13184-5. (PMID: 19708647)
      Biochemistry. 2007 May 1;46(17):5140-7. (PMID: 17407324)
      Nature. 2010 Apr 22;464(7292):1218-22. (PMID: 20376006)
      J Am Chem Soc. 2002 Sep 25;124(38):11270-1. (PMID: 12236732)
      Nucleic Acids Res. 2001 Mar 1;29(5):1097-106. (PMID: 11222759)
      Chembiochem. 2005 Nov;6(11):1960-2. (PMID: 16178037)
      J Biol Chem. 2010 Feb 19;285(8):5792-801. (PMID: 20007320)
      Structure. 2002 Aug;10(8):1063-72. (PMID: 12176384)
      Curr Opin Struct Biol. 2010 Dec;20(6):684-92. (PMID: 20951571)
      Biochemistry. 1997 Feb 11;36(6):1181-7. (PMID: 9063865)
      Proc Natl Acad Sci U S A. 2013 Jan 8;110(2):483-8. (PMID: 23267108)
      J Biol Chem. 2012 Nov 30;287(49):41174-85. (PMID: 23043105)
      Biochemistry. 2008 Oct 14;47(41):10999-1012. (PMID: 18803397)
      Biochemistry. 2009 Oct 6;48(39):9234-41. (PMID: 19711960)
      J Struct Biol. 1999 Apr-May;125(2-3):156-65. (PMID: 10222271)
      Angew Chem Int Ed Engl. 2012 Jul 27;51(31):7711-4. (PMID: 22715136)
      Nature. 2010 Jun 17;465(7300):891-6. (PMID: 20559380)
      J Biol Chem. 2010 Sep 10;285(37):28425-33. (PMID: 20584901)
    • Contributed Indexing:
      Keywords: Biosynthesis; Cofactor; Electron paramagnetic resonance; Iron–sulfur cluster; Ligand binding; Mössbauer spectroscopy; Pulsed EPR
    • Accession Number:
      0 (Buffers)
      023C2WHX2V (Tromethamine)
      7LP2MPO46S (S-Adenosylmethionine)
      EC 2.8.1.- (Sulfurtransferases)
    • Publication Date:
      Date Created: 20160605 Date Completed: 20170818 Latest Revision: 20181113
    • Publication Date:
      20231215
    • Accession Number:
      10.1007/s00775-016-1365-8
    • Accession Number:
      27259294