Dr. Kushal Sengupta - Katalytische Mechanismen bei Metalloenzymen


B.Sc. Jadavpur University, Kolkata, India (2008)
M.Sc. Jadavpur University, Kolkata, India (2010)
Ph.D. Indian Association for the Cultivation of Science, Kolkata, India (2016)
Postdoc Cornell University, USA (2016-2019)
Assistant Professor (in Chemistry) Abhedananda College under Burdwan University, India (Aug 2020 - March 2021)
Postdoc MPI CEC (April 2021 - Oct 2022)
Group Leader MPI CEC (since Nov 2022)

Full publications list | Google Scholar

Selected publications

# - equal contribution

  • Ahmed, M. E., Chattopadhyay, S., Chatterjee, S. and Sengupta, K. (2022). Oxygen reduction reaction in enzymatic biofuel cells. Oxygen Reduction Reaction, Elsevier: 427-466. (Book chapter) https://www.sciencedirect.com/science/article/pii/B9780323885089000082
  • Fu, B.#, Sengupta, K.#, Genova, L. A.#, Santiago, A. G., Jung, W., Krzemiński, Ł., Chakraborty, U. K., Zhang, W. and Chen, P. (2020). Metal-induced sensor mobilization turns on affinity to activate regulator for metal detoxification in live bacteria. Proceedings of the National Academy of Sciences 117(24), 13248-13255. https://www.pnas.org/doi/abs/10.1073/pnas.1919816117.
  • Sengupta, K., Chatterjee, S. and Dey, A. (2016). In Situ Mechanistic Investigation of O2 Reduction by Iron Porphyrin Electrocatalysts Using Surface-Enhanced Resonance Raman Spectroscopy Coupled to Rotating Disk Electrode (SERRS-RDE) Setup. ACS Catalysis 6(10), 6838-6852. https://pubs.acs.org/doi/full/10.1021/acscatal.6b01122
  • Sengupta, K., Chatterjee, S., Samanta, S., Bandyopadhyay, S. and Dey, A. (2013). Resonance Raman and electrocatalytic behavior of thiolate and imidazole bound iron porphyrin complexes on self-assembled monolayers: Functional modeling of cytochrome P450. Inorganic chemistry 52(4), 2000-2014. https://pubs.acs.org/doi/full/10.1021/ic302369v
  • Sengupta, K., Chatterjee, S., Samanta, S. and Dey, A. (2013). Direct observation of intermediates formed during steady-state electrocatalytic O2 reduction by iron porphyrins. Proceedings of the National Academy of Sciences 110(21), 8431-8436. https://www.pnas.org/doi/abs/10.1073/pnas.1300808110
  • Pramanik, D.#, Sengupta, K.#, Mukherjee, S., Dey, S. G. and Dey, A. (2012). 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. Journal of the American Chemical Society 134(29), 12180-12189. https://pubs.acs.org/doi/full/10.1021/ja303930f

  • 2021 Marie Skłodowska-Curie Actions Seal of Excellence, European Research Commission
  • 2020 Alexander von Humboldt fellowship, Germany
  • 2015 Society of Biological Inorganic Chemistry Travel award, ICBIC-17, China
  • 2014 SNIC Student Bursary, ICCC-41, Singapore
  • 2010 Council of Scientific & Industrial Research-National Eligibility Test award, India


Dr. Maria Alessandra Martini


Elena Marie Böhme
Nina Breuer
Christine Leenen
Patricia Malkowski
Michael Reus
Adrian van Wasen
News aus den BioLabs

July 2023

Mr. Gursahib Singh Sethi, from TIFR Mumbai, India,  joins the team. He will be pursuing his Ph.D. in our department. We wish him all the best!

Serena, Kushal, and Isis had a beamtime at the I20 scanning beamline at DLS. It was a very nice beamtime with very interesting observations.

The BioLabs went for their annual “Betriebsausflug” on the last day of July. This time it was an indoor golf tournament.

June 2023

Ms. Elena Marie Böhme joins BioLabs as a technician after completing her apprentice training at MPI CEC. We welcome Elena and look forward to working together.

May 2023

MPI CEC had an Open Day on 13th May. BioLabs saw a great turnout of people. Some pictures from the event.

April 2023

Kushal presents his work on Nitrogenase at BITS Pilani Goa, India. Thanks to Dr. Sudipta Chatterjee for the invitation.

March 2023

Laure represents BioLabs during Fachbeirat with a brilliant talk.

Feb 2023

Maria, Chris, and Kushal complete a very successful and fun beamtime at Diamond I20. They got assistance from former BioLabs members James and Patri. Thanks to Liqun for the constant online support.

Metalloenzyme Mechanistic Explorations

In Nature metalloenzymes carry out some of the most fundamental chemical reactions (including dinitrogen reduction to ammonia, hydrogen production, reduction of carbon monoxide/dioxide, methane oxidation to methanol etc.) at very high catalytic rates and with very high efficiency. In spite of the importance and pertinence of the above-mentioned chemical conversions in energy research, there are significant knowledge gaps in the mechanisms by which these enzymes carry out their respective reactions. In metalloenzyme catalysis, earth abundant metals are of special relevance as metalloenzymes use them in their active sites. Intrigued and inspired by these metalloenzymes, our group is trying to learn the role of metal active sites and their surrounding coordination spheres in the mechanism of the fundamental chemical transformations (Figure 1A), a particular focus is to generate and stabilize the intermediates involved in these transformations. We use a combination of biochemical, biophysical, electrochemical and spectroscopic (UV-Vis, IR, EPR, Mössbauer and X-ray based (XAS and XES)) techniques to provide a complete picture of the catalytic active site and the involvement of the neighboring residues and establish a structure-function relationship.

Figure 1. A) Examples of several chemical reactions and the respective metalloenzymes involved in performing them that our group is interested in. B) Crystal structure of (PDB id:4WZA) Mo Nitrogenase (Mo N2ase) from Azotobacter vinelandii, one of our proteins of interest. C) The two metal clusters and some of the important residues involved in the catalysis in Mo N2ase.


Almost every metalloenzyme, in addition to the catalytic active site, involves additional metal clusters/sites which act as structural sites or are involved in electron/substrate transfers to the active site. Some examples of the additional sites are the 4Fe-4S clusters in Hydrogenases or the unique 8Fe-7S cluster, known as the P-cluster, in N2ases (Figure 1B, C) in addition to the catalytic site (FeMo-co, Figure 1B, C). Moreover, metalloenzymes are often assisted by other metalloproteins for electron transfers and substrate (and co-substrate) diffusions. Our group recognizes the importance of these additional sites/metalloproteins and aims to study them for better understanding of biological catalysis.

A major limitation in studying many metalloenzymes is many times the lack of efficient/suitable heterologous expression systems for their purification. Additionally, their purification from native organisms is not only complicated and time taking but is also of low yield. This especially affects spectroscopic investigations such as X-ray based techniques because it can be very sample intensive.  In collaboration with Dr. Decamps group, our group is developing and optimizing recombinant expression systems of metalloenzymes, particularly sMMO, in order to have better yields. sMMO or soluble Methane Monooxygenase (Figure 2) is a metalloenzyme which activates O2 and inserts one atom into an unactivated C–H bond of methane to yield methanol (CH3OH). Our biochemical approaches will be key for enabling advanced spectroscopic studies within our group and more broadly within the Department of Inorganic Spectroscopy, which should ultimately shed light on the key catalytic intermediates in these important energy converting enzymes.

Figure 2. Crystal structure of the hydroxylase component of methane monooxygenase from Methylosinus trichosporium OB3b (PDB id: 1MHZ); the enlarged view of the diiron active site (right).

Open Positions

The “Metalloenzyme Mechanistic Explorations” (MeME) team is always looking for highly motivated and dedicated Bachelor, Master or PhD students and Postdoctoral researchers who are interested and would love to work with proteins and inorganic spectroscopy. If you wish to join the team, please contact Dr. Kushal Sengupta with your CV and cover letter.