Filiz, ErtuğrulKoç, İbrahimÖzyiğit, İbrahim İlker2020-04-302020-04-3020140273-22891559-0291https://doi.org/10.1007/s12010-014-0922-2https://hdl.handle.net/20.500.12684/3118Filiz, Ertugrul/0000-0001-9636-6389; Ozyigit, Ibrahim Ilker/0000-0002-0825-5951WOS: 000339103800013PubMed: 24781980Superoxide 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.en10.1007/s12010-014-0922-2info:eu-repo/semantics/closedAccessSuperoxide dismutaseAntioxidant proteinsBrachypodium distachyon3D modelingIn silico analysisArticle173511831196WOS:000339103800013Q2Q3