Seminar Details

Seminar Title
::
Engineering Ferritin Protein Cage to facilitate Iron Mobilization and to design it as an Artificial Nanoenzyme
Seminar Type
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Registration Seminar
Department
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Chemistry
Speaker Type
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Student
Speaker Name
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Narmada Behera (518CY1004),
Date  &  Time
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18 Sep 2020  4:30 PM
Venue
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Online Mode (Through MS Team) (code: a6xz9tu)
Contact
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2650
Abstract
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Iron, one of the most essential elements, is present in trace amounts (only ⁓ 4 grams) in our body. About 25% of the total body iron is present inside a hollow nanocage protein called “Ferritin”, which are mostly intracellular. Ferritin stores these iron in the form of ferrihydrite mineral in its central nanocavity and releases it in a controlled fashion for various cellular metabolic activities. However, the iron release mechanism, in vivo, remains unclear and debatable. Owing to the reducing nature of the cytosolic environment, the reductive mobilization of iron from ferritin justifies as one of the possible mechanism to mimic the iron release process, in vivo. This reductive approach uses physiological reducing agent, in combination with suitable electron relay molecules to facilitate iron mobilization, as these thick and stable ferritin cages limit the process. Therefore, the current work investigates the efficacy of three cytosolic reducing agents (NADH, GSH and Ascorbate) and the impact of quinones, as electron relay molecules, during reductive iron mobilization from ferritin. Whether these reducing agents/electron relay molecules diffuse across (enter) the protein shell to carry out direct mineral core reduction or participate in long-range electron transfer (ET) via protein shell to mobilize iron, also remains unclear and hence requires detailed investigation. These investigations wouldnot only strengthen our understanding of the ferritin iron release process, in vivo, but also hold importance in other biological ET processes and O2 based cellular toxicity. In addition, high thermal stability of ferritin nanocage would be exploited to engineer them as thermostable artificial nanoenzyme.