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.

• 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.