@article{MendelHercherZupoketal.2020,
  author    = {Mendel, Ralf R. and Hercher, Thomas W. and Zupok, Arkadiusz and Hasnat, Muhammad Abrar and Leimk{\"u}hler, Silke},
  title     = {The requirement of inorganic Fe-S clusters for the biosynthesis of the organometallic molybdenum cofactor},
  series = {Inorganics : open access journal},
  volume    = {8},
  journal   = {Inorganics : open access journal},
  number    = {7},
  publisher = {MDPI},
  address   = {Basel},
  issn      = {2304-6740},
  doi       = {10.3390/inorganics8070043},
  pages     = {23},
  year      = {2020},
  abstract  = {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.},
  language  = {en}
}
@article{TeraoGarattiniRomaoetal.2020,
  author    = {Terao, Mineko and Garattini, Enrico and Rom{\~a}o, Maria Jo{\~a}o and Leimk{\"u}hler, Silke},
  title     = {Evolution, expression, and substrate specificities of aldehyde oxidase enzymes in eukaryotes},
  series = {The journal of biological chemistry},
  volume    = {295},
  journal   = {The journal of biological chemistry},
  number    = {16},
  publisher = {American Society for Biochemistry and Molecular Biology},
  address   = {Rockville},
  issn      = {0021-9258},
  doi       = {10.1074/jbc.REV119.007741},
  pages     = {5377 -- 5389},
  year      = {2020},
  abstract  = {Aldehyde oxidases (AOXs) are a small group of enzymes belonging to the larger family of molybdo-flavoenzymes, along with the well-characterized xanthine oxidoreductase. The two major types of reactions that are catalyzed by AOXs are the hydroxylation of heterocycles and the oxidation of aldehydes to their corresponding carboxylic acids. Different animal species have different complements of AOX genes. The two extremes are represented in humans and rodents; whereas the human genome contains a single active gene (AOX1), those of rodents, such as mice, are endowed with four genes (Aox1-4), clustering on the same chromosome, each encoding a functionally distinct AOX enzyme. It still remains enigmatic why some species have numerous AOX enzymes, whereas others harbor only one functional enzyme. At present, little is known about the physiological relevance of AOX enzymes in humans and their additional forms in other mammals. These enzymes are expressed in the liver and play an important role in the metabolisms of drugs and other xenobiotics. In this review, we discuss the expression, tissue-specific roles, and substrate specificities of the different mammalian AOX enzymes and highlight insights into their physiological roles.},
  language  = {en}
}