Research

Iron is the most essential nutrient, but highly toxic when it’s free and in excess. Therefore, iron concentration is tightly regulated by Nature in almost all organisms using intracellular ferritin protein, for sequestration and repository purposes. Ferritin proteins are hollow, symmetrical, nanocaged spherical structures, self-assembled from 24-subunits and can accommodate up to 4500 iron atoms, unlike 4 atoms in haemoglobin. Iron enters the ferritin nanocavity through eight hydrophilic 3-fold ion channels. In human, about 1/4th of total body iron is safely stored inside ferritin nano cavity. When required, ferritin caged iron is used for cell metabolism such as synthesis of haemoglobin, DNA and ATP, but the process and rate of iron release in response to cellular requirement remains an unsolved puzzle. Finding the iron exit pathway/mechanism is our current focus to control and manipulate the iron extracting process. This research can be further extended to control microbial growth and improve iron chelation therapy. 

Selected Publications

9.   “Alteration of Coaxial Heme Ligands Reveals the Role of Heme in Bacterioferritin from Mycobacterium

       tuberculosis”.
       Mohanty A., Parida A., Subhadarshanee B., Behera, N., Subudhi, T., Koochana P. K., Behera, R.K*.
       Inorganic Chemistry; 2021, 60(22), 16937-16952.

8.   “Kinetics of Ferritin Self-assembly by Laser Light Scattering: Impact of Subunit Concentration, pH and Ionic
       Strength”. Mohanty A., Mithra K., Jena SS*, Behera, R.K*.
       Biomacromolecules; 2021, 22(4), 1389-1398.

7.    "Impact of Phosphate on Iron Mineralization and Mobilization in Non-heme Bacterioferritin B from
        Mycobacterium tuberculosis"
        Parida, A; Mohanty, A; Kansara, B; Behera, R.K*.
        Inorganic Chemistry; 2020, 59(1), 629-641.

6.   "Iron Mineralizing Bacterioferritin A from Mycobacterium tuberculosis exhibits Unique Catalase-Dps like
       Dual Activities".
       Mohanty, A; Subhadarshanee, B; Barman, P; Mahapatra, C; Aishwarya, B.; Behera, R.K*.
       Inorganic Chemistry; 2019, 58(8), 4741-4752.

5.   “Releasing Iron from Ferritin Protein Nanocage by Reductive Method: The Role of Electron Transfer
        Mediator.”
        Koochana PK, Mohanty A, Das S, Subhadarshanee B, Satpati S, Dixit A, Sabat SC, Behera R.K*.
        Biochimica et Biophysica Acta (BBA) – General Subjects.; 2018, 1862, 1190-1198.

4.    “Surface Charge Dependent Separation of Modified and Hybrid Ferritin in Native PAGE: Impact of
        Lysine 104”.
        Subhadarshanee B, Mohanty A, Jagdev MK, Vasudevan D, Behera R.K*.
        Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics.; 2017, 1865, 1267-73.

3.   “Solving Biology's Iron Chemistry Problem with Ferritin Protein Nanocages”
       Theil EC, Tosha T, Behera R.K.
       Accounts of Chemical Research.; 2016, 49, 784-91.

2.   “Moving Fe2+ from Ferritin Ion Channels to Catalytic OH Centers Depends on Conserved Protein Cage 
       Carboxylates.”
       Behera, R. K and Theil, E. C.
       Proc Natl Acad Sci (PNAS) USA,; 2014, 111(22), 7925-30.

1.  “Ferritins for Chemistry and for Life.”
      Theil, E. C., Behera, R. K., and Tosha, T
      Coordination Chemistry Reviews.; 2013, 257, 579-86.