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The Requirement of Inorganic Fe-S Clusters for the Biosynthesis of the Organometallic Molybdenum Cofactor

1
Institute of Plant Biology, Braunschweig University of Technology, Humboldtstr. 1, 38106 Braunschweig, Germany
2
Department of Molecular Enzymology, Institute of Biochemistry and Biology, University of Potsdam, Karl-Liebknecht-Str. 24-25, 14476 Potsdam, Germany
*
Author to whom correspondence should be addressed.
Received: 18 June 2020 / Revised: 14 July 2020 / Accepted: 14 July 2020 / Published: 16 July 2020
Iron-sulfur (Fe-S) clusters are essential protein cofactors. In enzymes, they are present either in the rhombic [2Fe-2S] or the cubic [4Fe-4S] form, where they are involved in catalysis and electron transfer and in the biosynthesis of metal-containing prosthetic groups like the molybdenum cofactor (Moco). Here, we give an overview of the assembly of Fe-S clusters in bacteria and humans and present their connection to the Moco biosynthesis pathway. In all organisms, Fe-S cluster assembly starts with the abstraction of sulfur from l-cysteine and its transfer to a scaffold protein. After formation, Fe-S clusters are transferred to carrier proteins that insert them into recipient apo-proteins. In eukaryotes like humans and plants, Fe-S cluster assembly takes place both in mitochondria and in the cytosol. Both Moco biosynthesis and Fe-S cluster assembly are highly conserved among all kingdoms of life. Moco is a tricyclic pterin compound with molybdenum coordinated through its unique dithiolene group. Moco biosynthesis begins in the mitochondria in a Fe-S cluster dependent step involving radical/S-adenosylmethionine (SAM) chemistry. An intermediate is transferred to the cytosol where the dithiolene group is formed, to which molybdenum is finally added. Further connections between Fe-S cluster assembly and Moco biosynthesis are discussed in detail. View Full-Text
Keywords: Moco biosynthesis; Fe-S cluster assembly; l-cysteine desulfurase; ISC; SUF; NIF; iron; molybdenum; sulfur Moco biosynthesis; Fe-S cluster assembly; l-cysteine desulfurase; ISC; SUF; NIF; iron; molybdenum; sulfur
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MDPI and ACS Style

Mendel, R.R.; Hercher, T.W.; Zupok, A.; Hasnat, M.A.; Leimkühler, S. The Requirement of Inorganic Fe-S Clusters for the Biosynthesis of the Organometallic Molybdenum Cofactor. Inorganics 2020, 8, 43. https://0-doi-org.brum.beds.ac.uk/10.3390/inorganics8070043

AMA Style

Mendel RR, Hercher TW, Zupok A, Hasnat MA, Leimkühler S. The Requirement of Inorganic Fe-S Clusters for the Biosynthesis of the Organometallic Molybdenum Cofactor. Inorganics. 2020; 8(7):43. https://0-doi-org.brum.beds.ac.uk/10.3390/inorganics8070043

Chicago/Turabian Style

Mendel, Ralf R.; Hercher, Thomas W.; Zupok, Arkadiusz; Hasnat, Muhammad A.; Leimkühler, Silke. 2020. "The Requirement of Inorganic Fe-S Clusters for the Biosynthesis of the Organometallic Molybdenum Cofactor" Inorganics 8, no. 7: 43. https://0-doi-org.brum.beds.ac.uk/10.3390/inorganics8070043

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