Veronika S. Karpushenkova

Ms. Veronika S. Karpushenkova

Belarusian State University, Minsk, Belarus
orcid

Research Focus & Metrics

Academic Career Length

5Years (2022-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

View All Publications
14 November 2022 in Chemistry Proceedings
Verified
Conference Paper
Open access
PDF file
VKVeronika S. Karpushenkova
Veronika S. Karpushenkova
LGLiliya Glinskaya
Liliya Glinskaya
YFYaroslav Faletrov
Yaroslav Faletrov
KBKseniia Bardakova
Kseniia Bardakova
YPYuliya A. Piskun
Yuliya A. Piskun
VSVladimir M. Shkumatov
Vladimir M. Shkumatov
There is a trend to find new ways of using photocatalysis in order to synthesize valuable products or to control or track live processes with special fluorescence-based molecular probes. The paper presents some results concerning new photochemical properties of azidoaniline, its 7-nitrobenzofurazan (NBD) derivative and ciprofloxacin derivatives.

23 December 2025 in bioRxiv
Verified
Preprint
Open access
AGAndrei Gilep
Andrei Gilep
CMChristopher MacCarthy
Christopher MacCarthy
TVTatsiana Varaksa
Tatsiana Varaksa
MKMarianna Karpova
Marianna Karpova
IGIrina Grabovec
Irina Grabovec
NSNatallia Strushkevich
Natallia Strushkevich
Analysis of drug-resistant strains of M.tuberculosis revealed a mutation in cytochrome P450 CYP143 gene located in the ESX-5 secretion cluster. The function of CYP143 is unknown. Available synteny information is insufficient to straightforwardly infer potential CYP143 substrates, because a full set of effector proteins/substrates exported by the ESX-5 secretion system has not yet been identified. Here we found that CYP143 is highly conserved among mycobacteria. We leverage the possible association of the G334A mutation in CYP143 with the development of resistance to test the frontline antitubercular drug rifampicin using purified proteins. Binding of rifampicin does not induce typical P450 spectral response, while the crystal structure at atomic resolution reveals the binding mode in the active site. The drug binds above the heme and adopts "closed" conformation of the ansa chain running almost parallel to the naphthoquinone core. In this conformation the oxygen atom bridging C12 and C29 of the macrocycle makes a hydrogen bond with a water molecule coordinating heme iron. The same binding mode was observed in crystal structures in complex with rifaximin, rifamycin S and two synthetic derivatives. In the ligand-bound state the protein retains an open conformation even in the presence of the redox partner, as evident from the crystal structure of the ternary complex. Despite binding close to the heme, no conversion was observed showing that either the rifamycins or the reduction system, or both, are insufficient to support a full catalytic cycle. These results pave the way to understand the development of rifampicin resistance/tolerance and the role of orphan CYPome of M.tuberculosis.