Print Email Facebook Twitter Substrate and cofactor binding to nitrile reductase Title Substrate and cofactor binding to nitrile reductase: A mass spectrometry based study Author Gjonaj, L. (TU Delft BT/Biocatalysis) Pinkse, M.W.H. Fernandez Fueyo, E. (TU Delft BT/Biocatalysis) Hollmann, F. (TU Delft BT/Biocatalysis) Hanefeld, U. (TU Delft BT/Biocatalysis) Date 2016-06-23 Abstract Nitrile reductases catalyse a two-step reduction of nitriles to amines. This requires the binding of two NADPH molecules during one catalytic cycle. For the nitrile reductase from E. coli (EcoNR) mass spectrometry studies of the catalytic mechanism were performed. EcoNR is dimeric and has no Rossman fold. It was demonstrated that during catalysis each active site binds one substrate molecule. NADPH binds independent of the substrate. The PreQ0 binding pocket of the active site is not involved in the binding of NADPH; this is in conflict with an earlier hypothesis. To reference this document use: http://resolver.tudelft.nl/uuid:66f75cad-72cd-4596-8dda-455528349502 DOI https://doi.org/10.1039/C6CY01140C ISSN 2044-4753 Source Catalysis Science & Technology Part of collection Institutional Repository Document type journal article Rights © 2016 L. Gjonaj, M.W.H. Pinkse, E. Fernandez Fueyo, F. Hollmann, U. Hanefeld Files PDF c6cy01140c.pdf 2.61 MB Close viewer /islandora/object/uuid:66f75cad-72cd-4596-8dda-455528349502/datastream/OBJ/view