Effect of metal Ions on the activity of ten NAD-dependent formate dehydrogenases

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dc.authoridHuri Bulut / 0000-0003-2706-9625en_US
dc.authorscopusidHuri Bulut / 57185264300
dc.authorwosidHuri Bulut / AAM-1432-2020
dc.contributor.authorBulut, Huri
dc.contributor.authorValjakka, Jarkko
dc.contributor.authorYüksel, Büşra
dc.contributor.authorYılmazer, Berin
dc.contributor.authorTurunen, Ossi
dc.contributor.authorBinay, Barış
dc.date.accessioned2020-10-16T12:41:32Z
dc.date.available2020-10-16T12:41:32Z
dc.date.issued2020en_US
dc.departmentİstinye Üniversitesi, Tıp Fakültesi, Temel Tıp Bilimleri Bölümüen_US
dc.description.abstractNAD-dependent formate dehydrogenase (FDH) enzymes are frequently used in industrial and scientific applications. FDH is a reversible enzyme that reduces the NAD molecule to NADH and produces CO2 by oxidation of the formate ion, whereas it causes CO2 reduction in the reverse reaction. Some transition metal elements - Fe3+, Mo6+ and W6 + - can be found in the FDH structure of anaerobic and archaeal microorganisms, and these enzymes require cations and other redox-active cofactors for their FDH activity. While NAD-dependent FDHs do not necessarily require any metal cations, the presence of various metal cations can still affect FDH activities. To study the effect of 11 different metal ions, NAD-dependent FDH enzymes from ten different microorganisms were tested: Ancylobacter aquaticus (AaFDH), Candida boidinii (CboFDH), Candida methylica (CmFDH), Ceriporiopsis subvermispora (CsFDH), Chaetomium thermophilum (CtFDH), Moraxella sp. (MsFDH), Myceliophthora thermophila (MtFDH), Paracoccus sp. (PsFDH), Saccharomyces cerevisiae (ScFDH) and Thiobacillus sp. (TsFDH). It was found that metal ions (mainly Cu2+ and Zn2+) could have quite strong inhibition effects on several enzymes in the forward reaction, whereas several cations (Li+, Mg2+, Mn2+, Fe3+ and W6+) could increase the forward reaction of two FDHs. The highest activity increase (1.97 fold) was caused by Fe3+ in AaFDH. The effect on the reverse reaction was minimal. The modelled structures of ten FDHs showed that the active site is formed by 15 highly conserved amino acid residues spatially settling around the formate binding site in a conserved way. However, the residue differences at some of the sites close to the substrate do not explain the activity differences. The active site space is very tight, excluding water molecules, as observed in earlier studies. Structural examination indicated that smaller metal ions might be spaced close to the active site to affect the reaction. Metal ion size showed partial correlation to the effect on inhibition or activation. Affinity of the substrate may also affect the sensitivity to the metal's effect. In addition, amino acid differences on the protein surface may also be important for the metal ion effect.en_US
dc.identifier.citationBulut, H., Valjakka, J., Yuksel, B., Yilmazer, B., Turunen, O., & Binay, B. (2020). Effect of Metal Ions on the Activity of Ten NAD-Dependent Formate Dehydrogenases. The protein journal, 10.1007/s10930-020-09924-x. Advance online publication. https://doi.org/10.1007/s10930-020-09924-xen_US
dc.identifier.doi10.1007/s10930-020-09924-xen_US
dc.identifier.pmid33043425en_US
dc.identifier.scopus2-s2.0-85092368137en_US
dc.identifier.scopusqualityN/Aen_US
dc.identifier.urihttps://doi.org/10.1007/s10930-020-09924-x
dc.identifier.urihttps://hdl.handle.net/20.500.12713/1141
dc.identifier.wosWOS:000576745100001en_US
dc.identifier.wosqualityQ4en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.indekslendigikaynakPubMeden_US
dc.institutionauthorBulut, Huri
dc.language.isoenen_US
dc.relation.ispartofProtein Jen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectMetal Ion Effecten_US
dc.subjectNAD-Dependent FDHen_US
dc.subjectReaction Kineticsen_US
dc.subjectStructural Analysisen_US
dc.titleEffect of metal Ions on the activity of ten NAD-dependent formate dehydrogenasesen_US
dc.typeArticleen_US

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