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

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...

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Veröffentlicht in:	Journal of biological inorganic chemistry 2016-07, Vol.21 (4), p.549-557
Hauptverfasser:	Molle, Thibaut, Clémancey, Martin, Latour, Jean-Marc, Kathirvelu, Velavan, Sicoli, Giuseppe, Forouhar, Farhad, Mulliez, Etienne, Gambarelli, Serge, Atta, Mohamed
Format:	Artikel
Sprache:	eng
Schlagworte:	Biochemistry Biochemistry, Molecular Biology Biomedical and Life Sciences Buffers Chemical Sciences Inorganic chemistry Life Sciences Microbiology Original Paper S-Adenosylmethionine - chemistry S-Adenosylmethionine - metabolism Sulfurtransferases - chemistry Sulfurtransferases - metabolism Thermotoga maritima - enzymology Tromethamine - chemistry
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