TIFR
Department of Chemical Sciences
School of Natural Sciences

S. Mazumdar

Shyamalava Mazumdar
Chairperson & Senior Professor
Department of Chemical Sciences
Office
:
Room D-319
Tata Institute of Fundamental Research, Homi Bhabha Road, Colaba
Mumbai 400 005
Phone
:
91 22 2278 2363/2533
Fax
:
91 22 2280 4610/4611
Email
:
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Academic Profile
Doctoral Degree
:
1990, T.I.F.R/University of Mumbai, Maharashtra, India
Postdoctoral Experience
:
1992-1993, Oxford University, UK.
  • Current Research
  • Selected Publications

We are involved in the study of structural and mechanistic aspects of the biochemical function of various electron transfer and redox metalloenzymes using different physicochemical techniques.

Studies on wild type, and specifically designed mutant proteins are being carried out in the laboratory. The metalloenzymes currently being studied are:cytochrome c oxidase, cytochrome P450 and peroxidases. We are involved in the study of Enzyme kinetics, Protein stability and unfolding-refolding processes, protein engineering etc.

The following main techniques are used in these studies:
  • Circular Dichroism
  • Stopped-Flow
  • Micro-Calorimetry
  • Protein Mass Spectrometry (ESI-MS & MALDI-MS)
  • Protein Engineering Techniques
  • High-Eesolution NMR and Time-Resolved Fluorescence
  • Nusrat J. M. Sanghamitra and Shyamalava Mazumdar
    Conformational Dynamics Coupled to Protonation Equilibrium at the CuA Site of Thermus thermophilus: Insights into the Origin of Thermostability
    Biochemistry, (2008) 47 (5), 1309 -1318
  • A. Sujak, Nusrat J. M. Sanghamitra, O. Maneg, B. Ludwig and Shyamalava Mazumdar Thermostability of proteins: Role metal binding and pH on the stability of the dinuclear CuA site of Thermus thermophilus Biophys. J. (2007) 93(8), 2845–2851
  • R. Murugan and Shyamalava Mazumdar
    Effect of Alcohols on Binding of Camphor to Cytochrome P450cam: Spectroscopic and Stopped Flow Transient Kinetic Studies
    Arch. Biochem. Biophys. (2006) 455(2), 154-162
  • Soumen Kanti Manna and Shyamalava Mazumdar
    Role of Threonine 101 on the stability of the heme active site of cytochrome P450cam: Multi-wavelength Circular Dichroism Studies
    Biochemistry (2006), 45(42), 12715 - 12722
  • R. Murugan and S. Mazumdar
    Structure of the heme centre and its redox properties in the C357M mutant of cytochrome P450cam ChemBioChem, (2005) 6, 1204-1211
  • Halan Prakash and S. Mazumdar
    Direct Correlation of the Crystal Structure of Proteins with the Maximum Positive and Negative Charge-States of Gaseous Protein Ions Produced by Electrospray Ionization
    J. Am. Soc. Mass Spectrom. (2005), 16, 1409-1421
  • R. Murugan and S. Mazumdar
    Role of substrate on the conformational stability of the heme active site of cytochrome P450cam: effect of temperature and low concentrations of denaturants
    J. Biol. Inorg. Chem. (2004), 9, 477-488
  • K. Chattopadhyay and S. Mazumdar
    Stabilization of partially folded states of cytochrome c in aqueous surfactant: effects of ionic and hydrophobic interactions
    Biochemistry (2003) , 42, 14606 - 14613
  • S. Gupta, A. Warne, M. Saraste, S. Mazumdar
    pH-induced conformational transition in the soluble CuA domain of Paracoccus denitrificans cytochrome oxidase.
    Biochemistry. 2001, 40(20):6180-9.
  • K. Chattopadhyay, S. Mazumdar
    Direct electrochemistry of heme proteins: effect of electrode surface modification by neutral surfactants.
    Bioelectrochemistry. 2001, 53(1):17-24.