publications

Ultrafast Dynamics of Hemin Aggregates on Femtosecond Time Scales Arpita Nath, J. A. Dharmadhikari, A. K. Dharmadhikari, D. Mathur, S Mazumdar
Phys. Chem. Chem. Phys., 2017, 19, 26862--26869

The protein inhibitor of nNOS (PIN/DLC1/LC8) binding does not inhibit the NADPH-dependent heme reduction in nNOS, a key step in NO synthesis Swapnil S. Parhad, Deepa Jaiswal, Krishanu Ray, Shyamalava Mazumdar
Biochem Biophys Res Commun (2016), 472, 189-193

Mono-nuclear copper complexes mimicking the intermediates for the binuclear copper center of the subunit II of cytochrome oxidase: a peptide based approach Dwaipayan Dutta Gupta, Dandamudi Usharani and Shyamalava Mazumdar
Dalton Trans., 2016, 45, 17624–17632

A molecular Fe-complex as a catalyst probe for in-gel visual detection of proteins via signal amplification Sushma Kumari, Chakadola Panda, Shyamalava Mazumdar and Sayam Sen Gupta Chem.
Commun (2015), 51, 15257-15260, DOI: 10.1039/C5CC04399A

Role of Substituents on the Reactivity and Product Selectivity in the Reactions of Naphthalene Derivatives Catalyzed by the Orphan Thermostable Cytochrome P450, CYP175A1 Shibdas Banerjee, Sandeep Goyal, and Shyamalava Mazumdar
Bioorganic Chemistry (2015) 62, 94–105

Regioselective Oxygenation of Polyunsaturated Fatty Acids by the Thermostable P450 from Thermus thermophilus HB27 Shibdas Banerjee, Dwaipayan Datta Gupta, and Shyamalava Mazumdar
Current Biotechnology, (2015), 4(3): 345 - 356 DOI: 10.2174/2211550104666150806202934

A molecular Fe-complex as a catalyst probe for in-gel visual detection of proteins via signal amplification Sushma Kumari, Chakadola Panda, Shyamalava Mazumdar and Sayam Sen Gupta Chem.
Commun (2015), 51, 15257-15260, DOI: 10.1039/C5CC04399A

Thermodynamic effects of the alteration of the axial ligand on the unfolding of the thermostable cytochrome c Rabindra Kumar Behera, Hiroshi Nakajima, Jitumani Rajbongshi, Yoshihito Watanabe, Shyamalava Mazumdar
Biochemistry (2013), 52(8), 1373–1384

Mechanism of copper incorporation in the subunit II of cytochrome c oxidase from Thermus thermophilus: Identification of intermediate species Manas Kumar Ghosh, Priyanka Basak, and Shyamalava Mazumdar
Biochemistry (2013), 52 , 4620−4635

Conformational properties of the bis-μ-(thiolato) dicopper center in cytochrome c oxidase J. Rajbongshi, M.K. Ghosh, N.J.M. Sanghamitra, S. Gupta, Shyamalava Mazumdar
Ind. J. Chem. Sec. A, (2012), 51A(01-02), 83-98

Electrospray Ionization Mass Spectrometry: A Technique to access the information beyond the molecular weight of the analyte Shibdas Banerjee and Shyamalava Mazumdar
Int. J. Anal. Chem. 2012 (2012), Article ID 282574, 40 pages

Sequence Specific Association of Tryptic Peptides with Multiwalled Carbon Nanotubes: Effect of Localization of Hydrophobic Residues Megha S. Deshpande and Shyamalava Mazumdar
Biomacromolecules, (2012), 13 (5), 1410–1419

Role of the Surface-Exposed Leucine 155 in the Metal Ion Binding Loop of the CuA Domain of Cytochrome c Oxidase from Thermus thermophilus on the Function and Stability of the Protein Manas Kumar Ghosh, Jitumani Rajbongshi, Debajani Basumatary, and Shyamalava Mazumdar
Biochemistry, (2012), 51 (12), 2443–2452

Selective Deletion of the Internal Lysine Residue from the Peptide Sequence by Collisional Activation Shibdas Banerjee, Shyamalava Mazumdar
J. Am. Soc. Mass Spectrom. (2012) 23, 1967-1980

Biochemical and Molecular Dynamic Simulation Analysis of a Weak Coiled Coil Association between Kinesin-II Stalks Harinath Doodhi, Swadhin Jana, Pavithra Devan, Shyamalava Mazumdar, Krishanu Ray
PloS ONE (2012) 10.1371/journal.pone.0045981

Oxygenation of Monoenoic Fatty Acids by CYP175A1, an Orphan Cytochrome P450 from Thermus thermophilus HB27 Sandeep Goyal, Shibdas Banerjee and Shyamalava Mazumdar
Biochemistry(2012), 51, 7880−7890

Structural Design of the Active Site for Covalent Attachment of the Heme tothe Protein Matrix: Studies on a Thermostable Cytochrome P450 Sandeep Goyal, Megha S. Deshpande, and Shyamalava Mazumdar
Biochemistry (2011), 50, 1042–1052

Interaction of gammaxene with site specific mutants of Cytochrome P450cam Saptaswa Sen, Soumen Kanti Manna & Shyamalava Mazumdar
Ind. J. Chem. Sec. A, (2011), 50, 438-446

Evidence of Molecular Fragmentation inside the Charged Droplets Produced by Electrospray Process Shibdas Banerjee, Halan Prakash and Shyamalava Mazumdar
J. Am. Soc. Mass Spectrom. (2011), 22(10), 1707-1717

Conjugation of Cytochrome c with hydrogen titanate nanotubes: novel conformational state with implications for apoptosis Moumita Ray, Sriparna Chatterjee, Tanmay Das, Somnath Bhattacharyya, Pushan Ayyub, Shyamalava Mazumdar
Nanotechnology (2011), 22, 415705, doi:10.1088/0957-4484/ 22/ 41/ 415705

Oxidation of Unnatural Substrates by Engineered Cytochrome P450cam Saptaswa Sen, Soumen Kanti Manna and Shyamalava Mazumdar In Iron-Containing Enzymes: Versatile Catalysts of Hydroxylation Reactions in Nature, Sam P de Visser and D Kumar (Eds.).
Royal Society of Chemistry, (2011), Chapter 10, 330-365

Effects of salts on the charge-state distribution and the structural basis of the most intense charge-state of the gaseous protein ions produced by electrospray ionization H. Prakash, B.T. Kansara and S. Mazumdar
Int J Mass Spectrom (2010), 289, 84–91

Thermodynamic basis of the thermostability of CYP175A1 from Thermus thermophilus Rabindra Kumar Behera and S. Mazumdar
Int J Biol Macromol (2010), 46, 412–418

Tuning the substrate specificity by engineering the active site of cytochrome P450cam: A rational approach Soumen Kanti Manna and S. Mazumdar
Dalton Trans., (2010), 39, 3115–3123

Direct Electrochemistry of Dinuclear CuA fragment from cytochrome c oxidase of T. thermophilus at surfactant modified glassy carbon electrode J. Rajbongshi, D K Das, S. Mazumdar
Electrochim. Acta (2010), 55, 4174–4179

Covalent linkage of CYP101 with the electrode enhances the electro-catalytic activity of the enzyme: Vectorial electron transport from the electrode S. D. Mhaske, M. Ray and Shyamalava Mazumdar
Inorganica Chimica Acta (2010), 363, 2804–2811

Modification of the heme active site to increase the peroxidase activity of thermophilic cytochrome P450: A rational approach R. K. Behera, S. Goyal and Shyamalava Mazumdar
J. Inorg. Biochem (2010), 104 1185–1194

Non-covalent dimers of the lysine containing protonated peptide ions in gaseous state: electrospray ionizationmass spectrometric study Shibdas Banerjee and Shyamalava Mazumdar
J. Mass Spectrom (2010), 45, 1212–1219

Structural Design of the Active Site for Covalent Attachment of the Heme tothe Protein Matrix: Studies on a Thermostable Cytochrome P450 Sandeep Goyal, Megha S. Deshpande, and Shyamalava Mazumdar
Biochemistry (2011), 50, 1042–1052

Succinylation of cytochrome c investigated by electrospray ionization mass spectrometry: Reactive lysine residues Halan Prakasha and Shyamalava Mazumdar
International Journal of Mass Spectrometry, (2009), 281, 1-2, 55-62

Roles of two surface residues near the access channel in the substrate recognition by cytochrome P450cam Rabindra Kumar Behera and Shyamalava Mazumdar
Biophys. Chem (2008), 135, 1–6

Inhibition of Bacterial Oxidases by Formamide and analogues Sayan Gupta and Shyamalava Mazumdar
Biol. Chem., (2008), 389(5), 599-607

Reversible inactivation of cytochrome P450 by alkaline earth metal ions: Auxiliary metal ion induced conformation change and formation of inactive P420 species in CYP101 Soumen K. Manna, Shyamalava Mazumdar
J. Inorg. Biochem. (2008), 5-6, 1312-1321

Effect of Polar Solvents on the Optical Properties of Water-dispersible Thiol-Capped Cobalt Nanoparticles Nusrat J M Sanghamitra and Shyamalava Mazumdar
Langmuir (2008), 24 (7), 3439-3445

Conformational dynamics coupled to protonation equilibrium at the CuA site of T. thermophilus: Insights into the origin of thermostability Nusrat J.M. Sanghamitra and Shyamalava Mazumdar
Biochemistry (2008) 47, 1309 - 1318

Protein encapsulation into mesoporous silica hosts Y. S. Chaudhary, S. K. Manna, Shyamalava Mazumdar, D Khushalani
Micropor. Mesopor. Mater. (2008), 109 (1-3), 535-541

Thermostability of proteins: Role metal binding and pH on the stability of the dinuclear CuA site of Thermus thermophilus A. Sujak, Nusrat J. M. Sanghamitra, O. Maneg, B. Ludwig and Shyamalava Mazumdar
Biophys. J. (2007) 93(8), 2845–2851

Effect of Alcohols on Binding of Camphor to Cytochrome P450cam: Spectroscopic and Stopped Flow Transient Kinetic Studies R. Murugan and Shyamalava Mazumdar
Arch. Biochem. Biophys. (2006) 455(2), 154-162

Role of Threonine 101 on the stability of the heme active site of cytochrome P450cam: Multi-wavelength Circular Dichroism Studies Soumen Kanti Manna and Shyamalava Mazumdar
Biochemistry (2006), 45(42), 12715 - 12722

Structure of the heme centre and its redox properties in the C357M mutant of cytochrome P450cam R. Murugan and S. Mazumdar
ChemBioChem, (2005) 6, 1204-1211

Direct Correlation of the Crystal Structure of Proteins with the Maximum Positive and Negative Charge-States of Gaseous Protein Ions Produced by Electrospray Ionization Halan Prakash and S. Mazumdar
J. Am. Soc. Mass Spectrom. (2005), 16, 1409-1421

Role of substrate on the conformational stability of the heme active site of cytochrome P450cam: effect of temperature and low concentrations of denaturants R. Murugan and S. Mazumdar
J. Biol. Inorg. Chem. (2004), 9, 477-488

A simple formalism on dynamics of proteins on potential energy landscapes R. Murugan and S. Mazumdar
Protein Science, (2004), 13, 487-493

Stabilization of partially folded states of cytochrome c in aqueous surfactant: effects of ionic and hydrophobic interactions K. Chattopadhyay and S. Mazumdar
Biochemistry (2003) , 42, 14606 - 14613

Effect of redox potential of the heme on the peroxidase activity of cytochrome b562 S. Mazumdar , S. L. Springs , G. L. McLendon
Biophys. Chem., (2003), 105, 263–268

An NMR and circular dichroism study of the interaction of thiocyanate with human and cross-linked hemoglobin: identification of Lys-a-99 as a possible dissociation linked binding site A. K. Sau, D. Currell , S. Mazumdar , S. Mitra
Biophys. Chem., (2003) ,106, 233–240

Stabilization of partially folded states of cytochrome c in aqueous surfactant: effects of ionic and hydrophobic interactions K. Chattopadhyay and S. Mazumdar
Biochemistry (2003) , 42, 14606 - 14613

Effect of redox potential of the heme on the peroxidase activity of cytochrome b562 S. Mazumdar , S. L. Springs , G. L. McLendon
Biophys. Chem., (2003), 105, 263–268

An NMR and circular dichroism study of the interaction of thiocyanate with human and cross-linked hemoglobin: identification of Lys-a-99 as a possible dissociation linked binding site A. K. Sau, D. Currell , S. Mazumdar , S. Mitra
Biophys. Chem., (2003) ,106, 233–240

Steady state and time-resolved fluorescence studies on wild type high potential iron proteins; holo- and apo- forms A.K. Sau, Chun-An Chen, J.A. Cowan, S. Mazumdar and S. Mitra
Biophys. J., (2001), 81(4), 2320-2330.

Interaction of surfactants with biomolecules and mimics S. Mazumdar
Handbook of Surfaces and Interfaces of Materials, (2001), Ed. H.C. Nalwa, Academic Press, Volume 5: Biointerfaces and Applications, Chapter 3 pp 73-128.

Direct Observation of Release of Cytochrome c from Lipid Encapsulated Protein by Peroxide and Superoxide: A Possible Mechanism for Drug Induced Apoptosis N. Das, S. Gupta and S. Mazumdar
Biochem. Biophys. Res. Comm., (2001), 286(2), 311-314.

pH induced conformational transition in the soluble CuA domain of Paracoccus denitrificans cytochrome oxidase S. Gupta, A. Warne, M. Saraste and S. Mazumdar
Biochemistry, (2001), 40, 6180-6189

Direct Electrochemistry of Hemeproteins: Effect of electrode modification by neutral Surfactants K. Chattopadhyay, and S. Mazumdar
Bioelectrochemistry, (2001), 53, 17-24

Redox Linked Conformational Change in Bovine Heart Cytochrome c Oxidase: Picosecond Time-resolved Fluorescence Studies of the Cyanide Complex T. K. Das and S. Mazumdar
Biophys. Chem., (2002), 98, 267-273.

Binding of camphor to Pseudomonas putida cytochrome P450cam : Steady state and picosecond time-resolved fluorescence studies S. Prasad, S. Mazumdar and S. Mitra
FEBS Letts., (2000), 477, 157-160.

Effect of adriamycin on the boundary lipid structure of cytochrome c oxidase: Picosecond time-resolved fluorescence depolarization studies T. K. Das and S. Mazumdar
Biophys. Chem., (2000), 86, 15-28

Structural and Conformational Stability of Horseradish Peroxidase: Effect of Temperature and pH K. Chattopadhyay and S. Mazumdar
Biochemistry, (2000) 39(1), 263-270.

Direct electrochemical oxidation of horseradish peroxidase: Cyclic Voltammetric and spectroelectrochemical studies K. Chattopadhyay and S. Mazumdar
New J. Chem., (1999) 2, 137-139.

Unfolding pathway of cytochrome c oxidase induced by ionic surfactants: Circular dichroism and picosecond time-resolved fluorescence studies T. K. Das & S. Mazumdar
Proc. Ind. Acad. Sci. (Chem. Sc.), (1998), 110, 479-490.

J- and H- aggregate of Porphyrins with Surfactants: Fluorescence, Stopped-flow and Electron-microscopic Studies (Invited Article) N.C. Maiti, S. Mazumdar and N. Periasamy
J. Porphyrins and Phthalocyanins, (1998), 2, 369- 376.

Characterization of a partially unfolded structure of cytochrome c induced by sodium dodecyl sulphate and the kinetics of its refolding T.K Das, S. Mazumdar and S. Mitra
Eur. J. Biochem., (1998), 254, 662-670.

J- and H- aggregate of porphyrin-surfactant complexes: Time-resolved fluorescence and other spectroscopic studies. N. C. Maiti, S. Mazumdar and N. Periasamy
J. Phys. Chem. B, (1998), 102, 1528-1538.

Dielectric relaxation study of glycine and valine in water mixture using picosecond time domain reflectometry M.P. Lokhande, S. Mazumdar and S.C. Mehrotra
Ind. J. Biochem. Biophys., (1997), 34, 385-390.

Direct electrochemistry of heme undecapeptide in aqueous micellar solutions: the effect of hydrophobicity and axial ligation on redox potential of heme. K. Chattopadhyay and S. Mazumdar
Current Science, (1997), 73, 65-68.

Steady state and picosecond time-resolved fluorescence studies on recombinant Bacillus megaterium cytochrome P450 heme domain. K.K. Khan, S. Mazumdar, S. Modi, M.J. Sutcliffe, G.C.K. Roberts and S. Mitra
Eur. J. Biochem., (1997), 244, 361-370.

Controlled J-aggregation of porphyrins by cationic surfactants. N. C. Maiti, S. Mazumdar and N. Periasamy
Current Science, (1996), 70, 997-999.

Spectroscopic and mechanistic studies of type-1 and type -2 copper sites in Pseudomonas aeruginosa azurin as obtained by addition of external ligands to mutant His46Gly. G. van Pounderoyen, C.R. Andrew, T.M. Loehr, J. Sanders-Loehr, S. Mazumdar, H.A.O. Hill and G.W. Canters
Biochemistry, (1996), 35, 1397-1407.

Selective denaturation of cytochrome c oxidase by ionic surfactants: depletion of both the heme a residues from the enzyme. T. K. Das and S. Mazumdar
Current Science , (1995), 69, 874-876.

Fluorescence Dynamics of Non-covalently linked porphyrin dimer and aggregates. N. C. Maiti, M. Ravikanth, S. Mazumdar, N. Periasamy
J. Phys. Chem., (1995), 99, 17192-17197.

Time-resolved fluorescence study of the single tryptophan in thiocyanate and azide derivatives of horseradish peroxidase: Implication for a pH-induced conformational change in the heme cavity. T. K. Das and S. Mazumdar
Proc. Indian Acad. Sci. (Chem. Sci.), (1995), 107, 505-518.

Heme CD as a probe for monitoring local structural changes in heme proteins: Alkaline transition in hemeproteins. T. K. Das, S. Mazumdar and S. Mitra
Proc. Ind. Acad. Sci. (Chem. Sci.), (1995), 107, 497-503.

Conformational substates of apoprotein of horseradish peroxidase in aqueous solution: A fluorescence dynamics study. T. K. Das and S. Mazumdar
J. Phys. Chem., (1995), 99, 13283-13290.

Dynamics of Porphyrin Molecules in Micelles: Picosecond Time-Resolved Fluorescence Anisotropy Studies. N. C. Maiti, S. Mazumdar and N. Periasamy
J. Phys. Chem., (1995), 99, 10708-10715.

Ion-ion mutual neutralization if N2+ with F- and other fluorine containing negative ions. S.V.K. Kumar, S. Mazumdar and S. K. Mitra
Chem. Phys. Lett., (1995), 237, 448-455.

pH-Induced Conformational Perturbation in Horseradish Peroxidase: Picosecond Tryptophan Fluorescence Studies on Native and Cyanide Modified Enzyme T. K.i Das and S. Mazumdar
Eur. J. Biochem., (1995), 227, 823-828.

Conformation change due to reduction of cytochrome c oxidase in lauryl maltoside: pico second time resolved tryptophan fluorescence studies on the native and heat modified enzyme T. K. Das and S. Mazumdar
Biochim. Biophys. Acta, (1994), 1209, 227-237.

The introduction of a negative charge in the hydrophobic patch of Pseudomonas aeruginosa azurin affects the electron self exchange rate. G. van Pounderoyen, S. Mazumdar, N. Hunt, H. A. O. Hill, G. W. Canters
Eur. J. Biochem., (1994), 222, 583-588.

Adenosine Triphosphate Synthesis Using an Electrochemically-driven Proton Pump Petter J. Dobson, H.Allen O. Hill, Peter A. Leigh, S. Mazumdar and Alex Y.Safranov
J. Chem. Soc. (Chem. Comm.), (1994), 807-808.

Cytochrome c Oxidase: The unique enzyme at the terminal step of electron transfer in the respiratory chain. S. Mazumdar
Current Science, (1994), 66(9), 650-655.

Time-resolved study of tryptophan fluorescence in vesicle reconstituted cytochrome oxidase: effect of redox transition. T. K. Das and S. Mazumdar
FEBS Letts., (1993), 336(2), 211-214.

Binding of cyanide and thiocyanate to manganese reconstituted myoglobin and formation of peroxide compound: Optical spectral, multinuclear NMR and kinetic studies. M. S. Mondal, S. Mazumdar and S. Mitra
Inorg. Chem., (1993), 32, 5362-5367.

Micelle-induced release of heme-NO from nitric oxide complex of myoglobin. T. K. Das, S. Mazumdar and S. Mitra
J. Chem. Soc. (Chem. Comm.), (1993), 1447-1448.

Biomimetic chemistry of hemes inside aqueous micelles S. Mazumdar and S. Mitra
Structure and Bonding, (1993), 81, 115-145.

Octaethyl porphyrinato heme complexes encapsulated inside aqueous detergent micelles: NMR and optical spectral studies. S. Mazumdar
J. Chem. Soc. (Dalton), (1991), 2091-2096.

Stability and characterization of iron(III) and iron(II) heme peptides encapsulated in aqueous detergent micelles: 1H NMR and UV-vis spectroscopic studies. S. Mazumdar, O. K. Medhi and S. Mitra
Inorg. Chem., (1991), 30, 700-705.

Proton nuclear magnetic resonance and optical spectra of six-co-ordinated high-spin (S=2) bis (tetrahydrofuran) (3,7,12,17-tetramethyl- 8,13- divinyl- porphyrin- 2,18- dipropionato) iron(II) encapsulated in aqueous detergent micelles. S. Mazumdar and O. K. Medhi
J. Chem. Soc. (Dalton), (1990), 2633-2636.

1H and 13C NMR studies on the structure of micelles encapsulating hemes in aqueous SDS solutions. S. Mazumdar
J. Phys. Chem., (1990), 94, 5947-5953.

Low-spin iron(III) porphyrins encapsulated in aqueous detergent micelles: 1 H and 15 N NMR studies. S. Mazumdar, O. K. Medhi and S. Mitra
J. Chem. Soc. (Dalton), (1990), 1057-1061.

Aggregation in five coordinated high-spin hemins: determination of solution structure by 1H NMR. S. Mazumdar and S. Mitra
J. Phys. Chem., (1990), 94, 561-566.

On the quantal identification of low-lying electronic states of CO2+ D. Mathur, V. R. Marathe and S. Mazumdar
J. Phys. B, (1989), 22, L385-L389.

How are S2+ ions formed in electron collisions with linear S=C=S? S. Mazumdar, S. V. K. Kumar, V. R. Marathe and D. Mathur
Rapid comm. in Mass. Spec., (1989), 3, 24-26.

Proton NMR, optical spectra and magnetic properties of four-coordinated intermediate-spin, five-coordinated high-spin and six-coordinated low-spin iron(II) hemes encapsulated in aqueous detergent micelles: model for hemoproteins. O. K. Medhi, S. Mazumdar and S. Mitra
Inorg. Chem., (1989), 28, 3243-3247.

Electronic spectral study of the aqua = hydroxo equilibrium of model iron(III) haems encapsulated in aqueous detergent micelles. S. Mazumdar, O. K. Medhi, N. Kannadaguili and S. Mitra
J. Chem. Soc. (Dalton), (1989), 1003-1005.

The CS2 dication. S. Mazumdar, V. R. Marathe, S. V. K. Kumar, and D. Mathur
Int. J. Mass. Spec. and Ion Processes, (1988) 86, 351-355.

SELECTED PAPERS PUBLISHED IN PROCEEDINGS OF INTERNATIONAL CONFERENCES

TConformational Stability of binuclear copper center in subunit II of cytochrome c Oxidase from Paracoccus denitrificans Proceedings of the XII international Biophysics Congress, September 19-24, 1999, New Delhi, India (published in Journal of Biosciences, Vol. 24, suppliment 1, page 73)

Conformational studies on the binuclear CuA site of Cytochrome c oxidase Proceedings of the 10th International Conference on Bioinorganic Chemistry (ICBIC-10), August 26-31, 2001, Florence, Italy (Abstract Published in Journal of Bioinorganic Chemistry, 86 (1): 72-72.

Effect of camphor on the stability of heme in Cytochrome P450cam: Urea mediated unfolding studies, Proceedings of Eleventh International Conference of Biological Inorganic Chemistry (ICBIC-11) held at Cairns, Australia During July 19 - 23 2003, Abstract Published In J. Biol.Inorg. Chem., 2003

Effect of the surrounding micro-environment on the reaction of the heme with peroxide Proceedings of International symposium on active oxygen-metal complexes (ISAOC2004) held at Awaji Yumebutai International Center, Hyogo, Japan during January 6-9, 2004.

Substrate binding and conformational stability of the active site in cytochrome P450cam Proceedings of the 3rd Asian Biological Inorganic Chemistry Conference (AsBIC-III) held at Nanjing, P.R. China, Oct. 31-Nov. 3, 2006

Conformational stability of the CuA center of cytochrome oxidase Proceedings of Thirteenth International Conference of Biological Inorganic Chemistry (ICBIC-13) held at Vienna, Austria during July 15 - 20 2007, abstract published in J. Biol.Inorg. Chem., Vol 12, Suppl 1, 2007

The purple CuA site of cytochrome c oxidase Proceedings of the Fourth Asian Biological Inorganic Chemistry Conference (AsBIC-IV), Jeju, Korea during No-vember 10 to 13, 2008.

Redox-Linked Conformational Changes in Cyto-chrome c Oxidase Proceedings of the UMRS International Conference in Asia 2008 (IUMRS-ICA 2008), Nagoya, Japan, during December 9-11, 2008

Substrate recognition and conformational stability of the active site in cytochrome P450cam Proceedings of Fourteenth International Conference of Biological Inorganic Chemistry (ICBIC-14) held at Nagoya, Japan during July 25 and 30, 2009

Probing the formation of the high-valent redox intermediate in thermostable cytochrome p450 by rational modification of the active site, Proceedings of the 5th Asian Biological Inorganic Chemistry Conference (AsBIC-5) held in Kaohsiung, Taiwan during November 2-5, 2010.

The bis-(thiolato) dicopper center in cytochrome c oxidase: effects of outer sphere interactions on the stability and structure of the metal center Proceedings of the 3rd Asian conference on Inorganic Chemistry, (ACCC3) held in New Delhi during October 17-20, 2011

In vitro study of ATP7B (Wilson’s Disease) protein function In the Annual INASL Conference at Chandigarh, March 2011 Published in the Journal of Clinical and Experimental Hepatology1 (1) (Supplement) 50- 51 (2011)

Artificial Metalloenzyme: An Approach to Green Chemistry In CRSI zonal meeting at NCL, Pune during may 13 & 14, 2011

The High-Valent Redox Intermediate in the Thermostable Cytochrome P450: Study of Rational Modification of the Active Site National Seminar on Inorganic Chemistry–2011 and The Celebration of 150th Birth Anniversary of Acharya P. C. Ray (NSIC-2011)

Structure and stability of the CuA center in the cytochrome c oxidase from Thermus thermophilus The 6th Asian Conference on Biological Inorganic Chemistry (AsBIC6) held in Hong Kong in November 5-8, 2012.

The origin of high stability of the heme active site and fatty acid hydroxylation by the thermostable cytochrome P450 In the 16th International Conference on BioInorganic Chemistry (ICBIC16) in Grenoble, France, on 22 to 26 July, 2013.

Role of non-bonded amino acids near the active site on the stability and function of the heme in cytochrome P450’ In Eigth International Conference on Porphyrins and Phthalocyanines (ICPP8) in Istanbul, Turkey, June 22-27, 2014.

The stability and reactivity of a thermostable Cytochrome P450: Role of non-bonded residues near the active site In the 7th Biological Inorganic Chemistry Conference in Gold Coast, Australiaduring November 30 to December 4, 2014.

Understanding the active site properties of an orphan Cytochrome P450 In the 17th International Conference on Biological Inorganic Chemistry (ICBIC17) in Beijing, China, in July 20-24, 2015.