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- W2036496378 abstract "Iron is sparingly soluble in water; therefore, iron-containing enzymes in marine organisms such as diatoms must have critical physiological roles to justify the use of such a precious resource. We have identified a putative heme peroxidase of unknown function, Tp 21683, from the published genome of the model diatom Thalassiosira pseudonana. Conserved domain analysis suggests Tp 21683 consists of an N-terminal kringle domain, likely involved in ligand binding and localization, and a C-terminal b-type heme peroxidase domain. To dissect the function of the two domains of Tp 21683, we have optimized recombinant expression in Escherichia coli and subsequent refolding and purification of the isolated kringle and peroxidase domains. We report preliminary studies to identify the ligand-binding and peroxidase turnover properties of Tp 21683 toward a better understanding of the physiological role of peroxidases in diatoms. We show by intrinsic tryptophan fluorescence that unlike canonical kringle domains from human plasminogen, the kringle domain of Tp 21683 does not show measurable binding to lysine. However, the kringle domain appears to bind to the oleic acid with a Kd of approximately 1 μM. The peroxidase domain is able to turn over hydrogen peroxide using both the nonphysiological electron donor ABTS and the aromatic compound guaiacol with kcat of approximately 40 min-1 and 4 min-1, respectively. These data are the first analysis of a recombinant peroxidase from a diatom, and provide a basis for further investigation of the range of possible ligands and chemical reactions catalyzed by Tp 21683." @default.
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- W2036496378 date "2015-01-01" @default.
- W2036496378 modified "2023-10-16" @default.
- W2036496378 title "Ligand-Binding and Substrate Turnover of a Heme Peroxidase from the Diatom Thalassiosira Pseudonana" @default.
- W2036496378 doi "https://doi.org/10.1016/j.bpj.2014.11.1239" @default.
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