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Enzymatic Systems with Homology to Nitrogenase: Biosynthesis of Bacteriochlorophyll and Coenzyme F430

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Metalloproteins

Part of the book series: Methods in Molecular Biology ((MIMB,volume 1876))

Abstract

Enzymes with homology to nitrogenase are essential for the reduction of chemically stable double bonds within the biosynthetic pathways of bacteriochlorophyll and coenzyme F430. These tetrapyrrole-based compounds are crucial for bacterial photosynthesis and the biogenesis of methane in methanogenic archaea. Formation of bacteriochlorophyll requires the unique ATP-dependent enzyme chlorophyllide oxidoreductase (COR) for the two-electron reduction of chlorophyllide to bacteriochlorophyllide. COR catalysis is based on the homodimeric protein subunit BchX2, which facilitates the transfer of electrons to the corresponding heterotetrameric catalytic subunit (BchY/BchZ)2. By analogy to the nitrogenase system, the dynamic switch protein BchX2 contains a [4Fe-4S] cluster that triggers the ATP-driven transfer of electrons onto a second [4Fe-4S] cluster located in (BchY/BchZ)2. The subsequent substrate reduction and protonation is unrelated to nitrogenase catalysis, with no further involvement of a molybdenum-containing cofactor. The biosynthesis of the nickel-containing coenzyme F430 includes the six-electron reduction of the tetrapyrrole macrocycle of Ni2+-sirohydrochlorin a,c-diamide to Ni2+-hexahydrosirohydrochlorin a,c-diamide catalyzed by CfbC/D. The homodimeric CfbC2 subunit carrying a [4Fe-4S] cluster shows close homology to BchX2. Accordingly, parallelism for the initial ATP-driven electron transfer steps of CfbC/D was proposed. Electrons are received by the dimeric catalytic subunit CfbD2, which contains a second [4Fe-4S] cluster and carries out the saturation of an overall of three double bonds in a highly orchestrated spatial and regioselective process. Following a short introduction to nitrogenase catalysis, this chapter will focus on the recent progress toward the understanding of the nitrogenase-like enzymes COR and CfbC/D, with special emphasis on the underlying enzymatic mechanism(s).

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Authors and Affiliations

  1. Institut für Mikrobiologie, Technische Universität Braunschweig, Braunschweig, Germany

    Jürgen Moser

  2. Institut für Pharmazeutische Wissenschaften, Albert-Ludwigs-Universität Freiburg, Freiburg, Germany

    Gunhild Layer

Authors
  1. Jürgen Moser
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  2. Gunhild Layer
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Correspondence to Jürgen Moser or Gunhild Layer .

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Editors and Affiliations

  1. Department of Molecular Biology and Biochemistry, University of California-Irvine, Irvine, CA, USA

    Yilin Hu

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Moser, J., Layer, G. (2019). Enzymatic Systems with Homology to Nitrogenase: Biosynthesis of Bacteriochlorophyll and Coenzyme F430. In: Hu, Y. (eds) Metalloproteins. Methods in Molecular Biology, vol 1876. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-8864-8_2

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  • DOI: https://doi.org/10.1007/978-1-4939-8864-8_2

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  • Publisher Name: Humana Press, New York, NY

  • Print ISBN: 978-1-4939-8863-1

  • Online ISBN: 978-1-4939-8864-8

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