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Chem Sci. 2016 Jul 01;7(7):4633-4643. doi: 10.1039/c6sc01140c. Epub 2016 Mar 30.

The auxiliary [4Fe-4S] cluster of the Radical SAM heme synthase from .

Chemical science

Melanie Kühner, Peter Schweyen, Martin Hoffmann, José Vazquez Ramos, Edward J Reijerse, Wolfgang Lubitz, Martin Bröring, Gunhild Layer

Affiliations

  1. Institute of Microbiology , Technische Universität Braunschweig , Spielmannstr. 7 , 38106 Braunschweig , Germany.
  2. Institute of Inorganic and Analytical Chemistry , Technische Universität Braunschweig , Hagenring 30 , 38106 Braunschweig , Germany.
  3. Institute of Biochemistry , Leipzig University , Brüderstraße 34 , 04103 Leipzig , Germany . Email: [email protected].
  4. Max Planck Institute for Chemical Energy Conversion , Stiftstr. 34-36 , 45470 Mülheim an der Ruhr , Germany.

PMID: 30155111 PMCID: PMC6013774 DOI: 10.1039/c6sc01140c

Abstract

The heme synthase AhbD catalyzes the oxidative decarboxylation of two propionate side chains of iron-coproporphyrin III to the corresponding vinyl groups of heme during the alternative heme biosynthesis pathway occurring in sulfate-reducing bacteria and archaea. AhbD belongs to the family of Radical SAM enzymes and contains two [4Fe-4S] clusters. Whereas one of these clusters is required for substrate radical formation, the role of the second iron-sulfur cluster is not known. In this study, the function of the auxiliary cluster during AhbD catalysis was investigated. Two single cluster variants of AhbD from

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