(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. Soc. 2020 (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 Ghosh. Formation 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. 46, 13171-13175, 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. Soc. 139, 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.Chem. 290, 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 Trans. 43, 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 Catalysis, 3, 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. Soc. 131 (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. Soc. 131 (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. Soc. 130 (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. Soc. 129 (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. Soc. 129 (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. Soc. 2006, 128(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. Soc. 125(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. Langmuir, 18(19), 7154-7157, 2002.