TY  - JOUR
A1  - Mendel, Ralf R.
A1  - Hercher, Thomas W.
A1  - Zupok, Arkadiusz
A1  - Hasnat, Muhammad Abrar
A1  - Leimkühler, Silke
T1  - The requirement of inorganic Fe-S clusters for the biosynthesis of the organometallic molybdenum cofactor
JF  - Inorganics : open access journal
N2  - 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 froml-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.
KW  - Moco biosynthesis
KW  - Fe-S cluster assembly
KW  - l-cysteine desulfurase
KW  - ISC
KW  - SUF
KW  - NIF
KW  - iron
KW  - molybdenum
KW  - sulfur
Y1  - 2020
U6  - https://doi.org/10.3390/inorganics8070043
SN  - 2304-6740
VL  - 8
IS  - 7
PB  - MDPI
CY  - Basel
ER  -