Peter-Leon Hagedoorn is an expert in  the mechanistic investigation of metalloenzymes such as ferritin and chlorite dismutase, and he pioneered a new approach for metalloproteomics, called MIRAGE. He is a tenured assistant professor of Biocatalysis at the Department of Biotechnology, TU Delft. Pursuing his interest in kinetic characterization of enzymes on complex substrates he advanced the use of enzyme calorimetry with chip based devices. Of special interest are microsecond timescale rapid mixing techniques, unique in the world, employed in a continuous flow UV-vis spectrophotometric device called Nanospec, and a rapid freeze hyperquench device called MHQ. These techniques are circa 100 times faster than commercial instruments, and both techniques have been very powerful in the discovery of novel transient intermediates in the heme enzyme chlorite dismutase (ACS catalysis) and Cu2+ binding to ATCUN/NTS motif peptides (Angewandte Chemie). In recent years Hagedoorn ventured together with prof. Hanefeld into enzyme immobilization and flow biocatalys using Mn2+ dependent aldolases and hydroxynitrile lyases as well as thermophilic glycosyl transferases and hydratases (including FeS cluster containing enzymes). He has published over 110 peer reviewed papers, with a clear focus on the elucidation of reaction mechanisms of (metallo-)enzymes and metalloproteomics.

Hagedoorn is a member of the editorial board of Analytical Biochemistry. He has been a board member of the Netherlands Biotechnology Society (NBV) from 2016-2019, which involved the organization of the Netherlands Biotechnology Conference in 2017, 2018 and 2019. In 2020 he was asked to join the board of the Biocatalysis division of the European Federation of Biotechnology, for which he recently became the secretary. Hagedoorn is a member of the scientific committee for the European Conference on Biotechnology (ECB) 2024. He represents the Netherlands in the management committee for the COST action FeSImmChemNet, for which he is one of the workgroup leaders.