Structural analysis of wild-type and Val120Thr mutant Candida boidinii formate dehydrogenase by X-ray crystallography

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dc.authoridDemirci, Hasan/0000-0002-9135-5397
dc.authoridGul, Mehmet/0000-0001-5513-1866
dc.authorwosidDemirci, Hasan/HJP-7731-2023
dc.contributor.authorGul, Mehmet
dc.contributor.authorYuksel, Busra
dc.contributor.authorBulut, Huri
dc.contributor.authorDeMirci, Hasan
dc.date.accessioned2024-05-19T14:41:38Z
dc.date.available2024-05-19T14:41:38Z
dc.date.issued2023
dc.departmentİstinye Üniversitesien_US
dc.description.abstractCandida boidinii NAD(+)- dependent formate dehydrogenase (CbFDH) has gained significant attention for its potential application in the production of biofuels and various industrial chemicals from inorganic carbon dioxide. The present study reports the atomic X-ray crystal structures of wild-type CbFDH at cryogenic and ambient temperatures, as well as that of the Val120Thr mutant at cryogenic temperature, determined at the Turkish Light Source 'Turkish DeLight'. The structures reveal new hydrogen bonds between Thr120 and water molecules in the active site of the mutant CbFDH, suggesting increased stability of the active site and more efficient electron transfer during the reaction. Further experimental data is needed to test these hypotheses. Collectively, these findings provide invaluable insights into future protein-engineering efforts that could potentially enhance the efficiency and effectiveness of CbFDH.en_US
dc.description.sponsorshipNSF Science and Technology Center grant [NSF-1231306]; 2232 International Fellowship for Outstanding Researchers Program of TUBITAK [118C270]; TUBITAKen_US
dc.description.sponsorshipHD acknowledges support from NSF Science and Technology Center grant NSF-1231306 (Biology with X-ray Lasers, BioXFEL). This publication has been produced benefiting from the 2232 International Fellowship for Outstanding Researchers Program of TUBITAK (Project No. 118C270). However, the entire responsibility for the publication belongs to the authors of the publication. The financial support received from TUBITAK does not mean that the content of the publication is approved in a scientific sense by TUBITAK.en_US
dc.identifier.doi10.1107/S2059798323008070
dc.identifier.endpage1017en_US
dc.identifier.issn2059-7983
dc.identifier.pmid37860962en_US
dc.identifier.scopus2-s2.0-85175742206en_US
dc.identifier.scopusqualityQ1en_US
dc.identifier.startpage1010en_US
dc.identifier.urihttps://doi.org10.1107/S2059798323008070
dc.identifier.urihttps://hdl.handle.net/20.500.12713/5137
dc.identifier.volume79en_US
dc.identifier.wosWOS:001098067400005en_US
dc.identifier.wosqualityN/Aen_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.language.isoenen_US
dc.publisherInt Union Crystallographyen_US
dc.relation.ispartofActa Crystallographica Section D-Structural Biologyen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.snmz20240519_kaen_US
dc.subjectFormate Dehydrogenasesen_US
dc.subjectCandida Boidiniien_US
dc.subjectProtein Engineeringen_US
dc.subjectX-Ray Crystallographyen_US
dc.subjectStructural Biologyen_US
dc.subjectStructural Dynamicsen_US
dc.subjectTurkish Light Sourceen_US
dc.subjectTurkish Delighten_US
dc.titleStructural analysis of wild-type and Val120Thr mutant Candida boidinii formate dehydrogenase by X-ray crystallographyen_US
dc.typeArticleen_US

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