Biochemical characterization of wild-type and mutant (Q9F and S21Y/V22D) iron oxidases isolated from Acidithiobacillus ferrooxidans M1

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dc.contributor.authorÇolak, Dilsat Nigar
dc.contributor.authorGüler, Halil İbrahim
dc.contributor.authorÇanakçı, Sabriye
dc.contributor.authorBelduz, Ali Osman
dc.date.accessioned2021-09-17T10:09:27Z
dc.date.available2021-09-17T10:09:27Z
dc.date.issued2016
dc.departmentAÇÜ, Sağlık Bilimleri Fakültesi, Beslenme ve Diyetetik Bölümüen_US
dc.descriptionWe would like to thank Karadeniz Technical University Research Foundation (grant no. 1055) for their financial support.en_US
dc.description.abstractIron oxidase, a member of the high potential iron-sulfur protein (HiPIP) family within the iron-sulfur cluster, was thought to be involved in the iron respiratory electron transport chain in Acidithiobacillus ferrooxidans. A. ferrooxidans M1 strain was isolated from Murgul copper mine. The iro gene of this bacterium encoding iron oxidase was cloned, and the complete nucleotide sequence was disclosed. The gene was cloned and overexpressed successfully. The highly conserved amino acid residues within the iron oxidase enzyme sequence were determined, and their Q9F and S21Y/V22D recombinants were created through site-directed mutagenesis. Wild-type and recombinant iron oxidase enzymes were purified and further characterized. The biochemical properties and kinetic parameters of wild-type and mutant enzymes were determined and compared. The optimal temperature of the wild-type enzyme was 25 degrees C, and maximal activity was observed at pH 4.0. The Km and Vmax values of wild-type enzyme were 0.27 +/- 0.09 mM and 0.083 +/- 0.01 mu mol/min/mg protein, respectively. Although the mutant enzymes were almost comparable to wild-type enzyme, their maximal activities moved from pH 4.0 to pH 3.5, and pH stability of S21Y/V22D mutant was improved compared to wild type.
dc.identifier.citationÇolak, D. N., Güler, H. İ., Çanakci, S., & Beldüz, A. O. (2016). Biochemical characterization of wild-type and mutant (Q9F and S21Y/V22D) iron oxidases isolated from Acidithiobacillus ferrooxidans M1. Turkish Journal of Biology, 40(1), 166-173.en_US
dc.identifier.doi10.3906/biy-1501-31
dc.identifier.endpage173en_US
dc.identifier.issue1en_US
dc.identifier.scopusqualityQ1
dc.identifier.startpage166en_US
dc.identifier.urihttps://hdl.handle.net/11494/3436
dc.identifier.volume40en_US
dc.identifier.wosqualityN/A
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.institutionauthorGüler, Halil İbrahim
dc.language.isoenen_US
dc.publisherTUBITAK Scientific & Technical Research Council Turkeyen_US
dc.relation.ispartofTurkish Journal of Biology
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectAcidophilicen_US
dc.subjectIron oxidaseen_US
dc.subjectAcidithiobacillus ferrooxidansen_US
dc.subjectSite-directed mutagenesisen_US
dc.titleBiochemical characterization of wild-type and mutant (Q9F and S21Y/V22D) iron oxidases isolated from Acidithiobacillus ferrooxidans M1en_US
dc.typeArticle

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