Shyamalava Mazumdar
Dept. of Chemical Sciences
 
Contact
Office

Room B 125
Tata Institute of Fundamental Research
Homi Bhabha Road, Colaba, Mumbai 400 005

Phone: 91 (0) 22 22782363

Fax: 91 (0) 22 22804610/4611

E-Mail: shyamal@tifr.res.in
Personal Homepage
Research Interests
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-resolution 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.