NADPH-dependent diflavin oxidoreductase 1

Definition:

NADPH-dependent reductase which is a central component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Transfers electrons from NADPH via its FAD and FMN prosthetic groups to the [2Fe-2S] cluster of CIAPIN1, another key component of the CIA machinery. In turn, this reduced cluster provides electrons for assembly of cytosolic iron-sulfur cluster proteins. It can also reduce the [2Fe-2S] cluster of CISD1 and activate this protein implicated in Fe/S cluster repair. In vitro can fully activate methionine synthase/MTR in the presence of soluble cytochrome b5/CYB5A.

References:

[1]. M J Paine, et al. Cloning and characterization of a novel human dual flavin reductase. J Biol Chem. 2000 Jan 14;275(2):1471-8. [Content Brief]

[2]. Daili J A Netz, et al. Tah18 transfers electrons to Dre2 in cytosolic iron-sulfur protein biogenesis. Nat Chem Biol. 2010 Oct;6(10):758-65. [Content Brief]

[3]. Robert D Finn, et al. Identification of a functionally impaired allele of human novel oxidoreductase 1 (NDOR1), NDOR1*1. Pharmacogenet Genomics. 2005 Jun;15(6):381-6. [Content Brief]

[4]. Lucia Banci, et al. Molecular view of an electron transfer process essential for iron-sulfur protein biogenesis. Proc Natl Acad Sci U S A. 2013 Apr 30;110(18):7136-41. [Content Brief]

[5]. Francesca Camponeschi, et al. Anamorsin/Ndor1 Complex Reduces [2Fe-2S]-MitoNEET via a Transient Protein-Protein Interaction. J Am Chem Soc. 2017 Jul 19;139(28):9479-9482. [Content Brief]

[6]. Horatiu Olteanu, et al. Redundancy in the pathway for redox regulation of mammalian methionine synthase: reductive activation by the dual flavoprotein, novel reductase 1. J Biol Chem. 2003 Oct 3;278(40):38310-4. [Content Brief]

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