Comparative Analysis and Modeling of Superoxide Dismutases (SODs) in Brachypodium distachyon L.

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dc.contributor.authorFiliz, Ertuğrul
dc.contributor.authorKoç, İbrahim
dc.contributor.authorÖzyiğit, İbrahim İlker
dc.date.accessioned2020-04-30T22:41:04Z
dc.date.available2020-04-30T22:41:04Z
dc.date.issued2014
dc.departmentDÜ, Çilimli Meslek Yüksekokulu, Bitkisel ve Hayvansal Üretim Bölümüen_US
dc.descriptionFiliz, Ertugrul/0000-0001-9636-6389; Ozyigit, Ibrahim Ilker/0000-0002-0825-5951en_US
dc.descriptionWOS: 000339103800013en_US
dc.descriptionPubMed: 24781980en_US
dc.description.abstractSuperoxide dismutase (SOD, EC 1.15.1.1) is an enzyme catalyzing the dismutation of superoxide radical to hydrogen peroxide and dioxygen. To date, four types of SODs - Cu/ZnSOD, MnSOD, FeSOD, and NiSOD - have been identified. In this study, SOD proteins of Brachypodium distachyon (L.) Beauv. were screened by utilization of bioinformatics approaches. According to our results, Mn/FeSODs and Cu/ZnSODs of B. distachyon were found to be in basic and acidic character, respectively. Domain analyzes of SOD proteins revealed that iron/manganese SOD and copper/zinc SOD were within studied SOD proteins. Based on the seconder structure analyzes, Mn/FeSODs and Cu/ZnSODs of B. distachyon were found as having similar sheets, turns and coils. Although helical structures were noticed in the types of Mn/FeSODs, no the type of Cu/ZnSODs were identified having helical structures. The predicted binding sites of Fe/MnSODs and Cu/ZnSODs were confirmed for having His-His-Asp-His and His-His-His-Asp-Ser residues with different positions, respectively. The 3D structure analyzes of SODs revealed that some structural divergences were observed in patterns of SODs domains. Based on phylogenetic analysis, Mn/FeSODs were found to have similarities whereas Cu/ZnSODs were clustered independently in phylogenetic tree.en_US
dc.identifier.doi10.1007/s12010-014-0922-2en_US
dc.identifier.endpage1196en_US
dc.identifier.issn0273-2289
dc.identifier.issn1559-0291
dc.identifier.issue5en_US
dc.identifier.scopusqualityQ2en_US
dc.identifier.startpage1183en_US
dc.identifier.urihttps://doi.org/10.1007/s12010-014-0922-2
dc.identifier.urihttps://hdl.handle.net/20.500.12684/3118
dc.identifier.volume173en_US
dc.identifier.wosWOS:000339103800013en_US
dc.identifier.wosqualityQ3en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakPubMeden_US
dc.indekslendigikaynakScopusen_US
dc.language.isoenen_US
dc.publisherSpringeren_US
dc.relation.ispartofApplied Biochemistry And Biotechnologyen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectSuperoxide dismutaseen_US
dc.subjectAntioxidant proteinsen_US
dc.subjectBrachypodium distachyonen_US
dc.subject3D modelingen_US
dc.subjectIn silico analysisen_US
dc.titleComparative Analysis and Modeling of Superoxide Dismutases (SODs) in Brachypodium distachyon L.en_US
dc.typeArticleen_US

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