Pia Ädelroth

Pia Ädelroth

Professor in Biochemistry

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Works at Department of Biochemistry and Biophysics
Telephone 08-16 41 83
Visiting address Svante Arrhenius väg 16
Room A 461
Postal address Institutionen för biokemi och biofysik 106 91 Stockholm


Bacterial respiratory enzymes and nitric oxide metabolism

In most respiration chains, reduction of a terminal electron acceptor is linked to the production of a trans-membrane proton gradient, essential for the survival of the organism. The bacterial nitric oxide reductases (NOR) are part of an anaerobic respiration pathway termed denitrification, where they reduce the toxic nitric oxide (NO) to nitrous oxide (N2O). NORs belong to the same enzyme super-family as the oxygen-reducing proton pumping heme-copper oxidases (HCuOs) such as cytochrome c oxidase in human mitochondria. Our research aims at elucidating the structure-function relationship, cross-reactivity, energy conservation, proton transfer mechanisms and evolution of the NO (and O2)-reducing heme-copper oxidases.

We are also involved in a collaboration project on the 'Architecture and functional dynamics of the cellular power plant' funded by the Knut and Alice Wallenberg foundation, see:


Group members

Johanna Vilhjalmsdottir, Postdoc

Sofia Appelgren, PhD student

Davinia Espejo, PhD student

Olga Fedotovskaya, PhD student

Mateusz Janczak, PhD student


Selected Publications

  • Zhou, S., Pettersson, P., Huang, J., Sjöholm, J., Sjöstrand, D., Pomès, R., Högbom, M., Brzezinski, P., Mäler, L., and Ädelroth, P. (2018)Proc. Natl. Acad. Sci. USA 115, p. 3048-3053.

  • Gonska, N., Young, D., Yuki, R., Okamoto, T., Hisano, T., Antonyuk, S., Hasnain, S. S., Muramoto, K., Shiro, Y., Tosha, T., Ädelroth, P. (2018) ‘Characterization of the quinol-dependent nitric oxide reductase from the pathogen Neisseria meningitidis, an electrogenic enzyme’, Scientific Reports 8, 3637.

  • Poiana, F., von Ballmoos, C., Gonska, N., Blomberg, M., Ädelroth, P., and Brzezinski, P. (2017) ‘Splitting of the O-O Bond at the heme-copper catalytic site of respiratory oxidases’, Science Adv., 3, :e170027.

  • ter Beek, J., Kahle, M., and Ädelroth, P. (2017) ‘Modulation of protein function in membrane mimetics: Characterization of P. denitrificans cNOR in nanodiscs or liposomes’, Biochim. Biophys. Acta-Biomembranes, 1859, p. 1951-1961.

  • Bhagi-Damodaran, A., Kahle, M., Shi, Y., Zhang, Y., Ӓdelroth, P., and Lu, Y. (2017) ‘Insights into how heme reduction potential modulates enzymatic activities of a myoglobin-based functional oxidase’, Angew. Chem., Int. Ed., 56, 6622-6626.

  • Arjona, D., Wikström, M. and Ädelroth, P. (2015) ‘NO is a potent inhibitor of cbb3-type heme-copper oxidases’, FEBS Lett. 589, 1214–1218. 

  • Ahn, Y. O., Mahinthichaichan, P., Lee, H. J., Ouyang, H., Kaluka, D., Yeh, S. Arjona, D., Rousseau, D. L., Tajkhorshid, E., Ädelroth, P. and Gennis, R. B. (2014) ‘Conformational coupling between the active site and residues within the KC-channel of the Vibrio cholerae cbb3-type oxygen reductase’, Proc. Natl. Acad. Sci. USA, 111, E4419-E4428. 

  • ter Beek, J., Krause, N., Reimann, J., Lachmann, P., and Ädelroth, P. (2013) ‘The Nitric-Oxide reductase from Paracoccus denitrificans uses a single proton pathway’, J. Biol. Chem., 288, 30626-30635.



Funding Sources

Our studies are supported by grants from the Swedish Research Council (VR) and the Faculty of sciences at Stockholm University.

Last updated: April 7, 2021

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