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Name : Somdatta Ghosh Dey

Department : School of Chemical Sciences
Designation : Professor
Contact : +91 33 2473 4971 (Ext:1376)
Email : icsgd@iacs.res.in


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Our group’s research involves investigation of structure-function correlation of redox active metal and cofactor bound peptides which have been related to several diseases like Alzheimer’s disease and type 2 diabetes. We use various spectroscopic tools to investigate the geometric and electronic structures of these active sites to gain insight into their reactivities. Of particular interest are the interactions of these aberrant species with other biological molecules and pathways that are physiologically relevant to a particular pathology.

 



Academic Profile

Academic Profile

B. Sc., Chemistry Honors, Presidency College, Kolkata.
M. Sc., Chemistry, Indian Institute of Technology, Kanpur
Ph. D., Chemistry, Stanford University


Group

Will be available soon.


Publication

Publications

 

(56) Pal, Ishita; Roy, Madhuparna; *Dey, Somdatta Ghosh. Interaction of ApoMyoglobin with Heme-Amylin complex. J. Inorg. Biochem. 2020 (Accepted).

(55) Singha, Asmita; Mondal, Arnab; Nayek, Abhijit; *Dey, Somdatta Ghosh; *Dey, Abhishek. Oxygen Reduction By Iron Porphyrins with Covalently Attached Pendent Phenol and Quinol. J. Am. Chem. Soc2020 (Accepted).

(54) Nath Arnab, K.; Ghatak Arnab, *Dey Abhishek, *Dey Somdatta Ghosh Intermediates Involved in Serotonin Oxidation Catalyzed by Cu bound Aβ Peptides Chemical Science 2020 (Accepted).

(53) Mukherjee Sudipta, Nayek Abhijit, Bhunia Sharmistha, *Dey Somdatta Ghosh, *Dey Abhishek Single Iron Porphyrin Shows pH Dependent Switch between “Push” and “Pull” Effects in Electrochemical Oxygen Reduction Inorganic Chemistry 59 (19), 14564-14576, 2020.

(52) Bhunia Sarmistha,  Rana Atanu, *Dey Somdatta Ghosh, *Ivancich Annabella, *Dey Abhishek  A designed second-sphere hydrogen-bond interaction that critically influences the O–O bond activation for heterolytic cleavage in ferric iron–porphyrin complexes Chemical Science 11 (10), 2681-2695, 2020.

(51)  Roy, Madhuparna; Nath, Arnab, K.; Pal, Ishita; *Dey, Somdatta Ghosh. Heme in Alzheimer’s Disease. Featured Article, Chem. Comm.56, 4505-4518, 2020.

(50) (50) Pal, Ishita; Roy, Madhuparna; *Dey, Somdatta Ghosh. Active-​site environment of Cu bound amyloid β and amylin peptides. J. Biol. Inorg. Chem. Invited Article in Special Issue “Metal Ions and Degenerative Diseases”, 24(8), 1245-1259 2019.

(49) Pal, Ishita;  Nath, Arnab, K;  Roy, Madhuparna; Seal, Manas; Ghosh, Chandradeep;  Dey, Abhshek;  *Dey Somdatta GhoshFormation of Compound I in Heme bound Aβ-peptides relevant to Alzheimer’s Disease Chemical Science 10, 8405-8410, 2019.

(48) Adelson, Charles N.; Johnston, Esther M.; Hilmer, Kimberly M.; Watts, Hope; Dey, Somdatta Ghosh; Brown, Doreen E.; Broderick, Joan B.; Shepard, Eric M.; Dooley, David M.; Solomon, Edward I. Characterization of the Preprocessed Copper Site Equilibrium in Amine Oxidase and Assignment of the Reactive Copper Site in Topaquinone Biogenesis. J. Am. Chem. Soc. 141(22), 8877-8890, 2019.

(48) Pal, Ishita; Roy, Madhuparna; *Dey, Somdatta Ghosh. Copper Active Sites of Amyloid β and Amylin Peptides. J. Biol. Inorg. Chem. Invited Article in Special Issue “Metal Ions and Degenerative Diseases”,  24 (8), 1245-1259, 2019.

(47) Nath, Arnab, K.; Ghosh, Chandradeep; Roy, Madhuparna; Seal, Manas; *Dey, Somdatta Ghosh. Nitrite Reductase Activity of Heme and Copper bound Aβ Peptides. Dalton Trans. Invited Article New Talent: Asia Pacific themed issue, 48 (21), 7451-7461, 2019.

(46) Amanulah, Sk.; Ghosh, Chandradeep; *Dey, Somdatta Ghosh; *Dey, Abhishek. “Heme Proteins - Structure and Function” A Book Chapter in Porphyrins for the 21st Century: Fundamentals (Volume 1), Wiley

(45) Sarkar, Ankita; Sengupta, Kushal; Chatterjee, Sudipta; Seal, Manas; Faller, Peter; *Dey, Somdatta Ghosh; *Dey, Abhishek. Metal Binding to Aβ Peptides Inhibits Interaction with Cytochrome c: Insights from Abiological Constructs. ACS Omega. 3(10), 13994-14003, 2018.

(44) Seal, Manas; *Dey, Somdatta Ghosh. Active-Site Environment of Copper-Bound Human Amylin Relevant to Type 2 Diabetes.  Inorg. Chem. 57, 129–138, 2018.

(43) Mukherjee, Soumya; Ghosh, Chandradeep; Seal, Manas; *Dey, Somdatta Ghosh. Copper induced spin state change of heme-​Aβ associated with Alzheimer's disease.  Dalton Trans. 4613171-13175, 2017.

(42) Mukherjee, Soumya; Kapp, Eugene A.; Lothian, Amber; Roberts, Anne M.; Vasil’ev, Yury V.; Boughton, Berin A.; Barnham, Kevin J.; Kok, W. Mei;  Hutton, Craig A.; Masters, Colin L.; Bush, Ashley I.; Beckman, Joseph S.; Dey, Somdatta Ghosh; Roberts Blaine R. Characterization and Identification of Dityrosine Cross-Linked Peptides Using Tandem Mass Spectrometry. Anal. Chem.89 (11), 6136–6145, 2017.

(41) Johnston, Esther M.; Carreira, Cintia; Dell'Acqua, Simone; Dey, Somdatta Ghosh; Pauleta, Sofia R.; Moura, Isabel; Solomon, Edward I. Spectroscopic Definition of the CuZo Intermediate in Turnover of Nitrous Oxide Reductase and Molecular Insight into the Catalytic Mechanism. J. Am. Chem. Soc139, 4462-4476, 2017.

(40) Seal, Manas; Mukherjee, Soumya; *Dey, Somdatta Ghosh Fe-​oxy adducts of heme-​Aβ and heme-​hIAPP complexes: intermediates in ROS generation. Metallomics 8, 1266-1272, 2016.

(39) *Dey, Abhishek; *Dey, Somdatta Ghosh. "Model Compounds for Nitric Oxide Reductase." A Book Chapter (Chapter 9, Model Compounds for Nitric Oxide Reductase) in Metalloenzymes in Denitrification: Applications and Environmental Impact, Isabel Moura , José J. G. Moura, Luísa Maia and Sofia R. Pauleta, Ed. Royal Society of Chemistry Pub., pp 185-224, 2016.

(38) Seal, Manas; Ghosh; Chandradeep; Basu, Olivia; *Dey Somdatta Ghosh Cytochrome c peroxidase activity of heme bound amyloid β peptides. J. Biol. Inorg. Chem.  21, 683-690, 2016.

(37) Ghosh, Chandradeep; Mukherjee, Soumya; Seal, Manas; *Dey Somdatta Ghosh Peroxidase to Cytochrome b Type Transition in the Active Site of Heme-Bound Amyloid β Peptides Relevant to Alzheimer’s Disease. Inorg. Chem. 55, 1748-1757, 2016.

(36) Ghosh, Chandradeep; Seal, Manas; Mukherjee, Soumya; *Dey, Somdatta Ghosh Alzheimer’s Disease: A Heme–Aβ Perspective. Acc. Chem. Res., 48, 2556-2564, 2015.

(35) Seal, M.; Uppal, S.; Kundu, S.; *Dey Somdatta Ghosh. Interaction of apoNeuroglobin with heme-​Aβ complexes relevant to Alzheimer's disease. J. Biol. Inorg. Chem.  20, 563-574, 2015.

(34) Uppal, S.; Salhotra, S.; Mukhi, N.; Zaidi, F. K.; Seal, M.; Dey Somdatta Ghosh; Bhat, R.; Kundu, S. Significantly Enhanced Heme Retention Ability of Myoglobin Engineered to Mimic the Third Covalent Linkage by Nonaxial Histidine to Heme (Vinyl) in Synechocystis Hemoglobin. J. Biol.Chem290, 1979-1993, 2015.

(33) Mukherjee, S.; Seal, M.; *Dey Somdatta Ghosh. Kinetics of serotonin oxidation by heme-​Aβ relevant to Alzheimer's disease. J. Biol. Inorg. Chem. 19, 1355-1365, 2014.

(32) Sengupta, K.; Chatterjee, S.; Pramanik, D.; *Dey Somdatta Ghosh; *Dey, Abhishek. Self-​assembly of stable oligomeric and fibrillar aggregates of Aβ peptides relevant to Alzheimer's disease: morphology dependent Cu​/heme toxicity and inhibition of PROS generation. Dalton Trans43, 13377-13383, 2014

(31) Sengupta, K.; Chatterjee, S.; Mukherjee, S.; *Dey Somdatta Ghosh; *Dey, Abhishek. Heme bound Amylin Self-Assembled Monolayers on Au Electrodes: An Efficient Bio-electrode for O2 Reduction to H2O. Chem. Comm., 50, 3806-3809, 2014.

(30) Pramanik, D.; Mukherjee, S.; *Dey Somdatta Ghosh. Apomyoglobin Sequesters Heme from Heme Bound Aβ Peptides. Inorg. Chem. 52, 10929–10935, 2013.

(29) Ghosh, Chandradeep; Mukherjee, Soumya; *Dey, Somdatta Ghosh. Direct Electron Transfer between Heme-Aβ and Cyt c: Possible Role in Alzheimer's Disease. Chem. Comm. 49, 5754-5756, 2013.

(28) Mukherjee, Soumya; *Dey, Somdatta, Ghosh. Heme Bound Amylin: Spectroscopic Characterization, Reactivity and Relevance to Type 2 Diabetes. Inorg. Chem. 52, 5226-5235, 2013.

(27) Ghosh, Chandradeep; *Dey, Somdatta, Ghosh. Ligand Field and Ligand Binding Analysis of the Active Site of Cu Bound Aβ Associated with Alzheimer's Disease. Inorg. Chem. 52, 1318-1327, 2013.

(26) Mondal, Biswajit; Sengupta, Kushal; Rana, Atanu; Mahammed, Atif; Botoshansky, Mark; *Dey, Somdatta Ghosh; *Gross, Zeev; *Dey, Abhishek. Cobalt Corrole Catalyst for Efficient Hydrogen Evolution Reaction from H2O under Ambient Conditions: Reactivity, Spectroscopy, and Density Functional Theory Calculations. Inorg. Chem. 52, 3381-3387, 2013.

(25) Dey, Subal; Rana, Atanu; *Dey, Somdatta Ghosh; *Dey, Abhishek. Electrochemical hydrogen production in acidic water by an azadithiolate bridged synthetic hydrogenese mimic: role of aqueous solvation in lowering overpotential. ACS Catalysis3, 429-436, 2013.

(24) Seal, Manas; Mukherjee, Soumya; Pramanik, Debajyoti; Mittra, Kaustuv; *Dey, Abhishek; *Dey, Somdatta, Ghosh. Analogues of Oxy-heme Aβ: Reactive Intermediates relevant to Alzheimer's Disease. Chem. Comm. 49, 1091-1093, 2013

(23) Ghosh, Chandradeep; Pramanik, Debajyoti; Mukherjee, Soumya; *Dey, Abhishek; *Dey, Somdatta, Ghosh. Interaction of NO with Cu and Heme-Bound Aβ Peptides Associated with Alzheimer's Disease. Inorg. Chem. 52, 362-368, 2013.

(22) Pramanik, Debajyoti; Ghosh, Chandradeep; Mukherjee, Soumya; *Dey, Somdatta, Ghosh.  Interaction of amyloid β peptides with redox active heme cofactor: Relevance to Alzheimer's disease. Coord. Chem. Rev. 257, 81-92, 2013.

(21) Pramanik, Debajyoti; Sengupta, Kushal; Mukherjee, Soumya; *Dey, Somdatta, Ghosh; *Dey, Abhishek. Self-Assembled Monolayers of Aβ peptides on Au Electrodes: An Artificial Platform for Probing the Reactivity of Redox Active Metals and Cofactors Relevant to Alzheimer's Disease. J. Am. Chem. Soc. 134, 12180-12189, 2012.

(20) Pramanik, Debajyoti; Chandradeep Ghosh, *Dey, Somdatta Ghosh. Heme-Cu Bound Aβ Peptides: Spectroscopic Characterization, Reactivity and Relevance to Alzheimer's Disease. J. Am. Chem. Soc. 133, 15545-15552, 2011.

(19)  Pramanik, Debajyoti; *Dey, Somdatta Ghosh. Active Site Environment of Heme-Bound Amyloid β Peptide Associated with Alzheimer's Disease. J. Am. Chem. Soc.133, 81-87, 2011.

(18) *Dey, Somdatta Ghosh, Dey, Abhishek. NO and O2 Reactivities of Functional Models of Nitric Oxide Reductase and Cytochrome c Oxidase. Dalton Trans. Persp. 40, 12633-12647, 2011.

(17) *Dey, Somdatta Ghosh; *Dey, Abhishek. "Application of Magnetic Circular Dichroism, X-Ray Absorption Spectroscopy and Extended X-Ray Absorption Fine Structure in determining the Geometric and Electronic Structure of Non-heme FeIV-oxo Intermediates and Synthetic Models." A Book Chapter in FeIV oxo oxidants: versatile hydrogen abstraction oxidants in nature, Samuel de Visser and Devesh Kumar, Ed. Royal Society of Chemistry Pub., 2011, 209-254.

(16)  Collman, James P.; Ghosh, Somdatta. Recent Applications of a Synthetic Model of Cytochrome c Oxidase:  Beyond Functional Modeling. Inorg. Chem. 49(13), 5798-5810, 2010. (Cover page article)

(15)  Collman, James P.; Ghosh, Somdatta; Dey, Abhishek; Decreau, Richard, A. Using a Functional Enzyme Model to Understand the Chemistry Behind Hydrogen Sulfide Induced Hibernation. Proc. Natl. Acad. Sci, U.S.A.106 (52), 22090-22095, 2009.

(14)  Collman, James P.; Dey, Abhishek; Barile, Christopher J.; Ghosh, Somdatta; Decreau, Richard. Inhibition of Electrocatalytic O2 Reduction of Functional CcO Models by Competitive, Non-Competitive, and Mixed Inhibitors. Inorg. Chem. 48, 10528-10534, 2009.

 (13)  Collman, James P.; Ghosh, Somdatta; Dey, Abhishek; Decreau, Richard, A.; Yang, Ying. Catalytic Reduction of O2 by Cytochrome c using a Synthetic Model of Cytochrome c Oxidase. J. Am. Chem. Soc131 (14), 5034-5035, 2009.

 (12)  Collman, James P.; Dey, Abhishek; Yang, Ying; Ghosh, Somdatta; Decreau, Richard, A. O2 reduction by a functional heme/nonheme bis-iron NOR model complex. Proc. Natl. Acad. Sci, U.S.A. 106 (26), 10528-10533, 2009.

 (11)  Ghosh, Somdatta; Xie, Xiangjin; Dey, Abhishek, Sun, Yan; Scholes, Charles, P.; Solomon, Edward I. Thermodynamic equilibrium between blue and green copper sites and the role of the protein in controlling function. Proc. Natl. Acad. Sci, U.S.A. 106 (13), 4969-4974, 2009.

 (10)  Ghosh, Somdatta; Dey, Abhishek; Sun, Yan; Scholes, Charles, P.; Solomon, Edward I. Spectroscopic and Computational Studies of Nitrite Reductase: Proton Induced Electron Transfer and Backbonding Contributions to Reactivity. J. Am. Chem. Soc131 (1), 277-288, 2009.

(9)  Collman, James P.; Yang, Ying; Dey, Abhishek; Decreau, Richard, A.;  Ghosh, Somdatta; Ohta, Takehiro; Solomon, Edward I. A functional nitric oxide reductase model. Proc. Natl. Acad. Sci, U.S.A. 105 (41), 15660-15665, 2008.

(8)  Ghosh, Somdatta; Cirera, Jordi, ; Vance, Michael; Ono, Tetsuya; Fujisawa, Kiyoshi, Solomon, Edward I. Spectroscopic and Electronic Structure Studies of Phenolate Cu(II) Complexes: Phenolate Ring Orientation and Activation Related to Cofactor Biogenesis. J. Am. Chem. Soc130 (48), 16262-16273, 2008.

(7)  Ghosh, Somdatta; Dey, Abhishek; Usov, Oleg M.; Sun, Yan; Grigoryants, Vladimir M.; Scholes. Charles .P; Solomon, Edward I. Resolution of the Spectroscopy vs. Crystallography issue for NO intermediates of Nitrite Reductase from Rhodobacter sphaeroides.  J. Am. Chem. Soc129 (34), 10310-10311, 2007.

(6)  Ghosh, Somdatta;  Gorelsky, Serge I.; George, Serena DeBeer;  Chan, Jeannine M.;  Cabrito, Ines; Dooley, David M.;  Moura, Jose J. G.; Moura, Isabel; Solomon, Edward I. Spectroscopic, Computational and Kinetic Studies of the μ4-Sulfide Bridged Tetranuclear CuZ Cluster in N2O Reductase: pH Effect on the Edge Ligand and its Contribution to Reactivity. J. Am. Chem. Soc129 (13), 3955-3965, 2007.

(5)  Solomon, Edward I.; Sarangi, Ritimuka; Woertink, Julia S.; Augustine, Anthony J.; Yoon, Jungjoo; Ghosh Somdatta. O2 and N2O Activation by Binuclear, Trinuclear, and Tetranuclear Cu Clusters in Biology. Acc. Chem. Res. 40(7), 581-591, 2007.

(4)  Gorelsky, Serge I.; Ghosh, Somdatta; Solomon, Edward I.   Mechanism of N2O Reduction by the μ4-S Tetranuclear CuZ Cluster of Nitrous Oxide Reductase.    J. Am. Chem. Soc2006128(1), 278-290.

(3)  Chen, Peng; Gorelsky, Serge I.; Ghosh, Somdatta; Solomon, Edward I.   N2O reduction by the μ4-sulfide-bridged tetranuclear CuZ cluster active site. Angew Chem. Int. Ed. 43(32), 4132-4140, 2004.

(2)  Ghosh, Somdatta; Gorelsky, Serge I.; Chen, Peng; Cabrito, Ines; Moura, Jose J. G.; Moura, Isabel; Solomon, Edward I.   Activation of N2O Reduction by the Fully Reduced μ4-Sulfide Bridged Tetranuclear CuZ Cluster in Nitrous Oxide Reductase.    J. Am. Chem. Soc125(51), 15708-15709, 2003.

(1)  Sangeetha, N. M.; Balasubramanian, R.; Maitra, Uday; Ghosh, Somdatta; Raju, A.R.   Novel Cationic and Neutral Analogues of Bile Acids: Synthesis and Preliminary Study of Their Aggregation Properties. Langmuir18(19), 7154-7157, 2002.