Author

Jan Zarzycki

Max Planck Institute for Terrestrial MicrobiologyORCID 0000-0002-6307-6497Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

Click to filter author papers

Biochemistry· 4

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 3 Organism:bacteria (other)· 1 Research Focus:cell type annotation· 1 Organism:plant (other)· 1 Approach:statistical model· 1

Frequent Co-Authors

Georg K. A. HochbergiD· 3 shared Nicole PacziaiD· 3 shared Simone PrinziD· 3 shared Tobias J. ErbiD· 3 shared Andreas M. KüffneriD· 2 shared Frederik V. SchmidtiD· 2 shared Johannes G. RebeleiniD· 2 shared P. Claus· 2 shared

Activity by Year

2025-2026 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 35 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

3 shared papersBiochemistry

Georg K. A. HochbergORCID

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Bottom-up reconstruction of minimal pyrenoids provides insights into the evolution and mechanisms of carbon concentration by EPYC1 proteins

Andreas M. Küffner, Bianca Pommerenke, L. Kley, J. Z. Y. Ng, S. Prinz, Matthias Tinzl, L. Schulz, P. Claus, Nicole Paczia, Tanguy Chotel, Melanie Klose, Jan Zarzycki, Georg K. A. Hochberg, Tobias J. Erb

The paper reconstructs minimal pyrenoids using EPYC1 proteins to study their evolution and carbon concentration mechanisms.

Nature Plants · Aug 14, 2026Peer-reviewedBiochemistry

Directed evolution of the Fe-nitrogenase for CO2 reduction to hydrocarbons

Niels N. Oehlmann, Frederik V. Schmidt, Jing Chen, Simone Prinz, Jan Zarzycki, Peter Claus, Jörg Kahnt, Tobias J. Erb, Johannes G. Rebelein

This study enhances Fe-nitrogenase's ability to convert CO2 to hydrocarbons through directed evolution, increasing CH4 production and expanding the product spectrum to include ethane and CO.

bioRxiv · Jul 9, 2026 · PreprintBiochemistry

Form IF Rubiscos include highly active, specific, and small subunit-independent enzymes.

Franziska Otto, Hendrik Westedt, Kevin P. Franzeck, Jan Zarzycki, Andreas M. Küffner, Luca Schulz, Simone Prinz, Nicole Paczia, P. Claus, Georg K. A. Hochberg, Tobias J. Erb

The paper identifies Form IF Rubiscos that are highly active, specific, and function without the small subunit, challenging the necessity of subunit complexity in Rubisco evolution.

bioRxiv · Mar 20, 2026 · PreprintBiochemistry

Methylthio-alkane reductases use nitrogenase metalloclusters for carbon-sulfur bond cleavage

Ana Lago-Maciel, Jéssica C. Soares, Jan Zarzycki, Charles J. Buchanan, Tristan Reif-Trauttmansdorff, Frederik V. Schmidt, Stefano Lometto, Nicole Paczia, Jan M. Schuller, D. Flemming Hansen, Gabriella T. Heller, Simone Prinz, Georg K. A. Hochberg, Antonio J. Pierik, Johannes G. Rebelein

This study presents the first molecular structure of methylthio-alkane reductase, revealing metalloclusters that inform its function and evolutionary relationship to nitrogenases.

Nature Catalysis · Oct 23, 2025Peer-reviewedBiochemistry