Name and Surname of the Supervisor: Mindaugas Lesanavičius
Institution (Company), Department: VU GMC BChI Ksenobiotikų biochemijos skyrius
Preliminary Topic: Kinetic and potentiometric characterization of mutant bacterial TrxR-type FNRs
Short Description of the Internship Work ): Ferredoxin:NADP+ oxidoreductases (FNRs, EC 1.18.1.2) are FAD containing flavoenzymes that catalyze electron transfer between ferredoxins and NADP+/NADPH thus being able to transform two-electron transfer into single-electron transfer. These enzymes participate in photosynthesis, nitrogen fixation, isoprenoid biosynthesis, xenobiotic detoxification, etc., and can be broadly classified into plant-type and glutathione reductase (GR) type FNRs. One of the subtypes of GR-type FNRs are poorly characterized thioredoxin reductase-type (TrxR) FNRs. They exhibit a homodimeric structure and a segmented FAD binding domain (the NADP(H) binding domain is inserted into the FAD binding domain. Moreover, they have a flexible C-terminal segment that covers the isoalloxazine ring of the bound FAD cofactor.
We have performed systematic studies of three bacterial TrxR-type FNRs from B. subtilis, C. tepidum and R. palustris over several years. A student is offered to perform steady- (UV/Vis spectrophotometry) and pre-steady-state (stopped-flow) kinetics with nonphysiological electron acceptors with B. subtilis and C. tepidum mutant variants (C-ter deletions) in order to elucidate the role of C- terminal in FNR catalysis.
Useful links: https://doi.org/10.3390/ijms27010481
Qualification Requirements (Degree): BSc
Application Deadline: 2027-01-31
Additional Comments: Biochemistry students preferred