Amplifying Reactivity of Bio-Inspired [FeFe]-Hydrogenase Mimics by Organic Nanotubes Md Estak Ahmed, Puspendu Das, Sk Mustak Ahamed, Samir Chattopadhyay, Abhijit Nayek, et al. Chemistry A European Journal, 2024 A bio‐inspired FeFe hydrogenase model which catalyses hydrogen evolution reaction (HER) in acidic solutions is immobilized in polyaniline (PANI)‐based nanotubes. A combination of analytical techniques reveals that this construct maintains both the molecular signatures of the bio‐inspired complex and the material properties of PANI. The amine and imine‐rich environment of the PANI chain amplifies the inherent HER activity of the bio‐inspired complex, allowing electrocatalytic HER at neutral pH, with lower overpotentials and higher current densities compared to the bio‐inspired complex alone. This construct retains the oxygen stability of the bio‐inspired complex and remains stable through several hours of aerobic electrolysis, producing only 6.5 % H₂O₂ from the competing oxygen reduction reaction (ORR).
Low Potential CO2 Reduction by Inert Fe(II)-Macrobicyclic Complex: A New Concept of Cavity Assisted CO2 Activation Piyali Sarkar, Sayan Sarkar, Abhijit Nayek, Nayarassery N. Adarsh, Arun K. Pal, et al. Small, 2024 The advantage of a pre‐organized π‐cavity of Fe(II) complex of a newly developed macrobicycle cryptand is explored for CO2 reduction by overcoming the problem of high overpotential associated with the inert nature of the cryptate. Thus, a bipyridine‐centered tritopic macrobicycle having a molecular π‐cavity capable of forming Fe(II) complex as well as potential for CO2 encapsulation is synthesized. The inert Fe(II)‐cryptate shows much lower potential in cyclic voltammetry than the Fe(II)‐tris‐dimethylbipyridine (Fe‐MBP) core. Interestingly, this cryptate shows electrochemical CO2 reduction at a considerably lower potential than the Fe‐MBP inert core. Therefore, this study represents that a well‐structured π‐cavity may generate a new series of molecular catalysts for the CO2 reduction reaction (CO2RR), even with the inert metal complexes.
Facile electrocatalytic proton reduction by a [Fe-Fe]-hydrogenase bio-inspired synthetic model bearing a terminal CN− ligand Abhijit Nayek, Subal Dey, Suman Patra, Atanu Rana, Pauline N. Serrano, et al. Chemical Science, 2024 An azadithiolate bridged CN− bound pentacarbonyl bis-iron complex, mimicking the active site of [Fe–Fe] H2ase is synthesized, which effectively reduces H+ to H2 between pH 0–3 at diffusion-controlled rates (1011 M−1 s−1) i.e. 108 s−1 at pH 3 with an overpotential of 140 mV.
Reduction of Sulfur Dioxide to Sulfur Monoxide by Ferrous Porphyrin** Aishik Bhattacharya, Arnab Kumar Nath, Arnab Ghatak, Abhijit Nayek, Souvik Dinda, et al. Angewandte Chemie International Edition, 2023 The reduction of SO2 to fixed forms of sulfur can address the growing concerns regarding its detrimental effect on health and the environment as well as enable its valorization into valuable chemicals. The naturally occurring heme enzyme sulfite reductase (SiR) is known to reduce SO2 to H2S and is an integral part of the global sulfur cycle. However, its action has not yet been mimicked in artificial systems outside of the protein matrix even after several decades of structural elucidation of the enzyme. While the coordination of SO2 to transition metals is documented, its reduction using molecular catalysts has remained elusive. Herein reduction of SO2 by iron(II) tetraphenylporphyrin is demonstrated. A combination of spectroscopic data backed up by theoretical calculations indicate that FeIITPP reduces SO2 by 2e−/2H+ to form an intermediate [FeIII−SO]+ species, also proposed for SiR, which releases SO. The SO obtained from the chemical reduction of SO2 could be evidenced in the form of a cheletropic adduct of butadiene resulting in an organic sulfoxide.
Second-Sphere Hydrogen-Bond Donors and Acceptors Affect the Rate and Selectivity of Electrochemical Oxygen Reduction by Iron Porphyrins Differently Arnab Ghatak, Soumya Samanta, Abhijit Nayek, Sudipta Mukherjee, Somdatta Ghosh Dey, et al. Inorganic Chemistry, 2022 The factors that control the rate and selectivity of 4e-/4H+ O2 reduction are important for efficient energy transformation as well as for understanding the terminal step of respiration in aerobic organisms. Inspired by the design of naturally occurring enzymes which are efficient catalysts for O2 and H2O2 reduction, several artificial systems have been generated where different second-sphere residues have been installed to enhance the rate and efficiency of the 4e-/4H+ O2 reduction. These include hydrogen-bonding residues like amines, carboxylates, ethers, amides, phenols, etc. In some cases, improvements in the catalysis were recorded, whereas in some cases improvements were marginal or nonexistent. In this work, we use an iron porphyrin complex with pendant 1,10-phenanthroline residues which show a pH-dependent variation of the rate of the electrochemical O2 reduction reaction (ORR) over 2 orders of magnitude. In-situ surface-enhanced resonance Raman spectroscopy reveals the presence of different intermediates at different pH's reflecting different rate-determining steps at different pH's. These data in conjunction with density functional theory calculations reveal that when the distal 1,10-phenanthroline is neutral it acts as a hydrogen-bond acceptor which stabilizes H2O (product) binding to the active FeII state and retards the reaction. However, when the 1,10-phenanthroline is protonated, it acts as a hydrogen-bond donor which enhances O2 reduction by stabilizing FeIII-O2.- and FeIII-OOH intermediates and activating the O-O bond for cleavage. On the basis of these data, general guidelines for controlling the different possible rate-determining steps in the complex multistep 4e-/4H+ ORR are developed and a bioinspired principle-based design of an efficient electrochemical ORR is presented.
Bioinorganic Chemistry on Electrodes: Methods to Functional Modeling Abhijit Nayek, Md Estak Ahmed, Soumya Samanta, Souvik Dinda, Suman Patra, et al. Journal of the American Chemical Society, 2022 One of the major goals of bioinorganic chemistry has been to mimic the function of elegant metalloenzymes. Such functional modeling has been difficult to attain in solution, in particular, for reactions that require multiple protons and multiple electrons (nH+/ne-). Using a combination of heterogeneous electrochemistry, electrode and molecule design one may control both electron transfer (ET) and proton transfer (PT) of these nH+/ne- reactions. Such control can allow functional modeling of hydrogenases (H+ + e- → 1/2 H2), cytochrome c oxidase (O2 + 4 e- + 4 H+ → 2 H2O), monooxygenases (RR'CH2 + O2 + 2 e- + 2 H+ → RR'CHOH + H2O) and dioxygenases (S + O2 → SO2; S = organic substrate) in aqueous medium and at room temperatures. In addition, these heterogeneous constructs allow probing unnatural bioinspired reactions and estimation of the inner- and outer-sphere reorganization energy of small molecules and proteins.
A Bidirectional Bioinspired [FeFe]-Hydrogenase Model Md Estak Ahmed, Abhijit Nayek, Alenka Križan, Nathan Coutard, Adina Morozan, et al. Journal of the American Chemical Society, 2022 With the price-competitiveness of solar and wind power, hydrogen technologies may be game changers for a cleaner, defossilized, and sustainable energy future. H2 can indeed be produced in electrolyzers from water, stored for long periods, and converted back into power, on demand, in fuel cells. The feasibility of the latter process critically depends on the discovery of cheap and efficient catalysts able to replace platinum group metals at the anode and cathode of fuel cells. Bioinspiration can be key for designing such alternative catalysts. Here we show that a novel class of iron-based catalysts inspired from the active site of [FeFe]-hydrogenase behave as unprecedented bidirectional electrocatalysts for interconverting H2 and protons efficiently under near-neutral aqueous conditions. Such bioinspired catalysts have been implemented at the anode of a functional membrane-less H2/O2 fuel cell device.
Second sphere control of CO2 reduction selectivity by iron porphyrins: The role of spin state S Patra, S Ghosh, S Samanta, A Nayek, A Dey Journal of Organometallic Chemistry 1023, 123439 , 2025 2025 Citations: 10
Amplifying Reactivity of Bio‐Inspired [FeFe]‐Hydrogenase Mimics by Organic Nanotubes ME Ahmed, P Das, SM Ahamed, S Chattopadhyay, A Nayek, M Mondal, ... Chemistry–A European Journal 30 (68), e202403011 , 2024 2024 Citations: 2
Hydrogen Oxidation by Bioinspired Models of [FeFe]-Hydrogenase A Nayek, RK Poria, ME Ahmed, S Patra, SG Dey, A Dey ACS Organic & Inorganic Au 5 (2), 105-116 , 2024 2024 Citations: 2
Phenoxide coordination to Fe (III) tetraphenylporphyrin: Exploring antibacterial and electrocatalytic HER activity M Patra, TK Das, A Saha, T Das, A Patra, S Garai, A Nayek, UK Roy, ... Inorganica Chimica Acta 568, 122084 , 2024 2024 Citations: 3
Low Potential CO 2 Reduction by Inert Fe(II)‐Macrobicyclic Complex: A New Concept of Cavity Assisted CO 2 Activation P Sarkar, S Sarkar, A Nayek, NN Adarsh, AK Pal, A Datta, A Dey, P Ghosh Small 20 (10), 2304794 , 2024 2024 Citations: 4
Facile electrocatalytic proton reduction by a [Fe–Fe]-hydrogenase bio-inspired synthetic model bearing a terminal CN− ligand A Nayek, S Dey, S Patra, A Rana, PN Serrano, SJ George, SP Cramer, ... Chemical Science 15 (6), 2167-2180 , 2024 2024 Citations: 13
Reduction of sulfur dioxide to sulfur monoxide by ferrous porphyrin A Bhattacharya, A Kumar Nath, A Ghatak, A Nayek, S Dinda, R Saha, ... Angewandte Chemie International Edition 62 (10), e202215235 , 2023 2023 Citations: 8
Second-Sphere Hydrogen-Bond Donors and Acceptors Affect the Rate and Selectivity of Electrochemical Oxygen Reduction by Iron Porphyrins Differently A Ghatak, S Samanta, A Nayek, S Mukherjee, SG Dey, A Dey Inorganic Chemistry 61 (33), 12931-12947 , 2022 2022 Citations: 16
Bioinorganic chemistry on electrodes: methods to functional modeling A Nayek, ME Ahmed, S Samanta, S Dinda, S Patra, SG Dey, A Dey Journal of the American Chemical Society 144 (19), 8402-8429 , 2022 2022 Citations: 10
A bidirectional bioinspired [FeFe]-hydrogenase model ME Ahmed, A Nayek, A Križan, N Coutard, A Morozan, S Ghosh Dey, ... Journal of the American Chemical Society 144 (8), 3614-3625 , 2022 2022 Citations: 59
Biochemical and artificial pathways for the reduction of carbon dioxide, nitrite and the competing proton reduction: effect of 2 nd sphere interactions in catalysis S Amanullah, P Saha, A Nayek, ME Ahmed, A Dey Chemical Society Reviews 50 (6), 3755-3823 , 2021 2021 Citations: 160
Oxygen reduction by iron porphyrins with covalently attached pendent phenol and quinol A Singha, A Mondal, A Nayek, SG Dey, A Dey Journal of the American Chemical Society 142 (52), 21810-21828 , 2020 2020 Citations: 75
A single iron porphyrin shows pH dependent switch between “Push” and “Pull” effects in electrochemical oxygen reduction S Mukherjee, A Nayek, S Bhunia, SG Dey, A Dey Inorganic Chemistry 59 (19), 14564-14576 , 2020 2020 Citations: 20
Induction of enzyme-like peroxidase activity in an iron porphyrin complex using second sphere interactions S Bhakta, A Nayek, B Roy, A Dey Inorganic Chemistry 58 (5), 2954-2964 , 2019 2019 Citations: 31
Alkoxy group facilitated ring closing metathesis A NAYEK, S BANERJEE, S SINHA, S GHOSH Tetrahedron letters 45 (34) , 2004 2004
MOST CITED SCHOLAR PUBLICATIONS
Biochemical and artificial pathways for the reduction of carbon dioxide, nitrite and the competing proton reduction: effect of 2 nd sphere interactions in catalysis S Amanullah, P Saha, A Nayek, ME Ahmed, A Dey Chemical Society Reviews 50 (6), 3755-3823 , 2021 2021 Citations: 160
Oxygen reduction by iron porphyrins with covalently attached pendent phenol and quinol A Singha, A Mondal, A Nayek, SG Dey, A Dey Journal of the American Chemical Society 142 (52), 21810-21828 , 2020 2020 Citations: 75
A bidirectional bioinspired [FeFe]-hydrogenase model ME Ahmed, A Nayek, A Križan, N Coutard, A Morozan, S Ghosh Dey, ... Journal of the American Chemical Society 144 (8), 3614-3625 , 2022 2022 Citations: 59
Induction of enzyme-like peroxidase activity in an iron porphyrin complex using second sphere interactions S Bhakta, A Nayek, B Roy, A Dey Inorganic Chemistry 58 (5), 2954-2964 , 2019 2019 Citations: 31
A single iron porphyrin shows pH dependent switch between “Push” and “Pull” effects in electrochemical oxygen reduction S Mukherjee, A Nayek, S Bhunia, SG Dey, A Dey Inorganic Chemistry 59 (19), 14564-14576 , 2020 2020 Citations: 20
Second-Sphere Hydrogen-Bond Donors and Acceptors Affect the Rate and Selectivity of Electrochemical Oxygen Reduction by Iron Porphyrins Differently A Ghatak, S Samanta, A Nayek, S Mukherjee, SG Dey, A Dey Inorganic Chemistry 61 (33), 12931-12947 , 2022 2022 Citations: 16
Facile electrocatalytic proton reduction by a [Fe–Fe]-hydrogenase bio-inspired synthetic model bearing a terminal CN− ligand A Nayek, S Dey, S Patra, A Rana, PN Serrano, SJ George, SP Cramer, ... Chemical Science 15 (6), 2167-2180 , 2024 2024 Citations: 13
Second sphere control of CO2 reduction selectivity by iron porphyrins: The role of spin state S Patra, S Ghosh, S Samanta, A Nayek, A Dey Journal of Organometallic Chemistry 1023, 123439 , 2025 2025 Citations: 10
Bioinorganic chemistry on electrodes: methods to functional modeling A Nayek, ME Ahmed, S Samanta, S Dinda, S Patra, SG Dey, A Dey Journal of the American Chemical Society 144 (19), 8402-8429 , 2022 2022 Citations: 10
Reduction of sulfur dioxide to sulfur monoxide by ferrous porphyrin A Bhattacharya, A Kumar Nath, A Ghatak, A Nayek, S Dinda, R Saha, ... Angewandte Chemie International Edition 62 (10), e202215235 , 2023 2023 Citations: 8
Low Potential CO 2 Reduction by Inert Fe(II)‐Macrobicyclic Complex: A New Concept of Cavity Assisted CO 2 Activation P Sarkar, S Sarkar, A Nayek, NN Adarsh, AK Pal, A Datta, A Dey, P Ghosh Small 20 (10), 2304794 , 2024 2024 Citations: 4
Phenoxide coordination to Fe (III) tetraphenylporphyrin: Exploring antibacterial and electrocatalytic HER activity M Patra, TK Das, A Saha, T Das, A Patra, S Garai, A Nayek, UK Roy, ... Inorganica Chimica Acta 568, 122084 , 2024 2024 Citations: 3
Amplifying Reactivity of Bio‐Inspired [FeFe]‐Hydrogenase Mimics by Organic Nanotubes ME Ahmed, P Das, SM Ahamed, S Chattopadhyay, A Nayek, M Mondal, ... Chemistry–A European Journal 30 (68), e202403011 , 2024 2024 Citations: 2
Hydrogen Oxidation by Bioinspired Models of [FeFe]-Hydrogenase A Nayek, RK Poria, ME Ahmed, S Patra, SG Dey, A Dey ACS Organic & Inorganic Au 5 (2), 105-116 , 2024 2024 Citations: 2
Alkoxy group facilitated ring closing metathesis A NAYEK, S BANERJEE, S SINHA, S GHOSH Tetrahedron letters 45 (34) , 2004 2004