Structural insights into the NAD+-dependent formate dehydrogenase mechanism revealed from the NADH complex and the formate NAD+ ternary complex of the Chaetomium thermophilum enzyme

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dc.authoridHuri Bulut / 0000-0003-2706-9625en_US
dc.authorscopusidHuri Bulut / 57185264300
dc.authorwosidHuri Bulut / AAM-1432-2020
dc.contributor.authorYılmazer, Berin
dc.contributor.authorIsupov, Michail N.
dc.contributor.authorDe Rose, Simone Antonio
dc.contributor.authorBulut, Huri
dc.contributor.authorBenninghoff, Jens C.
dc.contributor.authorBi?nay, Barış
dc.contributor.authorLittlechild, Jennifer Ann
dc.date.accessioned2020-11-05T12:08:36Z
dc.date.available2020-11-05T12:08:36Z
dc.date.issued2020en_US
dc.departmentİstinye Üniversitesi, Tıp Fakültesi, Temel Tıp Bilimleri Bölümüen_US
dc.description.abstractThe removal of carbon dioxide from the waste streams of industrial processes is a major challenge for creation of a sustainable circular economy. This makes the synthesis of formate from CO2 by NAD+ dependent formate dehydrogenases (FDHs) an attractive process for this purpose. The efficiency of this reaction is however low and to achieve a viable industrial process an optimised engineered enzyme needs to be developed. In order to understand the detailed enzymatic mechanism of catalysis structures of different cofactor and substrate complexes of the FDH from the thermophilic filamentous fungus, Chaetomium thermophilum have been determined to 1.2–1.3 Å resolution. The substrate formate is shown to be held by four hydrogen bonds in the FDH catalytic site within the ternary complex with substrate and NAD+and a secondary formate binding site is observed in crystals soaked with substrate. Water molecules are excluded from the FDH catalytic site when the substrate is bound. The angle between the plane of the NAD+ cofactor pyridine ring and the plane of the formate molecule is around 27°. Additionally, structures of a FDH mutant enzyme, N120C, in complex with the reduced form of the cofactor have also been determined both in the presence and absence of formate bound at the secondary site. These structures provide further understanding of the catalytic mechanism of this fungal enzyme.en_US
dc.identifier.citationYilmazer, B., Isupov, M. N., De Rose, S. A., Bulut, H., Benninghoff, J. C., Binay, B., & Littlechild, J. A. (2020). Structural insights into the NAD+-dependent formate dehydrogenase mechanism revealed from the NADH complex and the formate NAD+ ternary complex of the Chaetomium thermophilum enzyme. Journal of Structural Biology, 107657.en_US
dc.identifier.doi10.1016/j.jsb.2020.107657en_US
dc.identifier.issue3en_US
dc.identifier.pmid33148525en_US
dc.identifier.scopus2-s2.0-85094591210en_US
dc.identifier.scopusqualityN/Aen_US
dc.identifier.urihttps://doi.org/10.1016/j.jsb.2020.107657
dc.identifier.urihttps://hdl.handle.net/20.500.12713/1171
dc.identifier.volume212en_US
dc.identifier.wosWOS:000600997800021en_US
dc.identifier.wosqualityQ3en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.indekslendigikaynakPubMeden_US
dc.institutionauthorBulut, Huri
dc.language.isoenen_US
dc.publisherAcademic Press Inc.en_US
dc.relation.ispartofJournal of Structural Biologyen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectCatalytic Mechanismen_US
dc.subjectMutagenesisen_US
dc.subjectOxidoreductaseen_US
dc.subjectX-ray Crystallographyen_US
dc.titleStructural insights into the NAD+-dependent formate dehydrogenase mechanism revealed from the NADH complex and the formate NAD+ ternary complex of the Chaetomium thermophilum enzymeen_US
dc.typeArticleen_US

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