Tyrosine-specific bioconjugation allowing hole hopping along
aromatic chains of glucose oxidase

J 2025

Tyrosine-specific bioconjugation allowing hole hopping along aromatic chains of glucose oxidase

VECELYTE, Guoda; Vygaile DUDKAITE; Ondrej ŠEDO; Zbyněk ZDRÁHAL; Gintautas BAGDZIUNAS et al.

Základní údaje

Originální název

Tyrosine-specific bioconjugation allowing hole hopping along aromatic chains of glucose oxidase

Autoři

VECELYTE, Guoda; Vygaile DUDKAITE; Ondrej ŠEDO; Zbyněk ZDRÁHAL a Gintautas BAGDZIUNAS

Vydání

Materials Horizons, Royal Society of Chemistry, 2025, 2051-6347

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Velká Británie a Severní Irsko

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 10.700 v roce 2024

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:14740/25:00142824

Organizační jednotka

Středoevropský technologický institut

Klíčová slova anglicky

Tyrosine-specific bioconjugation; Glucose oxidase modification; Redox-active bioconjugates; Phenothiazine-5-oxide

Štítky

143160, CF PROT, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 24. 3. 2026 09:45, Mgr. Eva Dubská

Anotace

V originále

The potential of bioconjugated glucose oxidase enzymes for bioelectronic applications has been revealed in this research. By selectively modifying the enzyme with redox-active groups, we aimed to enhance the electrochemical properties of the enzyme while maintaining its biocatalytic activity. The phenothiazin-5-oxide and phenoxazine groups were selectively bioconjugated to the tyrosine residues on the enzyme surface. This bioconjugation was confirmed by mass spectrometry after enzymatic digestion of the protein. The self-assembly monolayer of modified enzyme exhibited improved bioelectrochemical behaviour, with enhanced anodic currents compared to the native enzyme. Marcus theory-based theoretical calculations revealed that hole hopping through the internal residues and from the electrode to the bioconjugated residues of the enzyme is thermodynamically favourable. The rate-limiting step for the bioelectrocatalytic process was identified as hole injection from the electrode to the bioconjugated enzyme surface. These findings demonstrate the potential of bioconjugated glucose oxidase for single molecule-based biosensing and bioelectronics.

Návaznosti

90242, velká výzkumná infrastruktura

Název: CIISB III

Citovat

VECELYTE, Guoda; Vygaile DUDKAITE; Ondrej ŠEDO; Zbyněk ZDRÁHAL a Gintautas BAGDZIUNAS. Tyrosine-specific bioconjugation allowing hole hopping along aromatic chains of glucose oxidase. Materials Horizons. Royal Society of Chemistry, 2025, roč. 12, č. 16, s. 6301-6309. ISSN 2051-6347. Dostupné z: https://doi.org/10.1039/d5mh00520e.

@article{2537977,
   author = {Vecelyte, Guoda and Dudkaite, Vygaile and Šedo, Ondrej and Zdráhal, Zbyněk and Bagdziunas, Gintautas},
   article_number = {16},
   doi = {https://doi.org/10.1039/d5mh00520e},
   keywords = {Tyrosine-specific bioconjugation; Glucose oxidase modification; Redox-active bioconjugates; Phenothiazine-5-oxide},
   language = {eng},
   issn = {2051-6347},
   journal = {Materials Horizons},
   title = {Tyrosine-specific bioconjugation allowing hole hopping along aromatic chains of glucose oxidase},
   url = {https://pubs.rsc.org/en/content/articlelanding/2025/mh/d5mh00520e},
   volume = {12},
   year = {2025}
}

TY  - JOUR
ID  - 2537977
AU  - Vecelyte, Guoda - Dudkaite, Vygaile - Šedo, Ondrej - Zdráhal, Zbyněk - Bagdziunas, Gintautas
PY  - 2025
TI  - Tyrosine-specific bioconjugation allowing hole hopping along aromatic chains of glucose oxidase
JF  - Materials Horizons
VL  - 12
IS  - 16
SP  - 6301-6309
EP  - 6301-6309
PB  - Royal Society of Chemistry
SN  - 20516347
KW  - Tyrosine-specific bioconjugation
KW  - Glucose oxidase modification
KW  - Redox-active bioconjugates
KW  - Phenothiazine-5-oxide
UR  - https://pubs.rsc.org/en/content/articlelanding/2025/mh/d5mh00520e
N2  - The potential of bioconjugated glucose oxidase enzymes for bioelectronic applications has been revealed in this research. By selectively modifying the enzyme with redox-active groups, we aimed to enhance the electrochemical properties of the enzyme while maintaining its biocatalytic activity. The phenothiazin-5-oxide and phenoxazine groups were selectively bioconjugated to the tyrosine residues on the enzyme surface. This bioconjugation was confirmed by mass spectrometry after enzymatic digestion of the protein. The self-assembly monolayer of modified enzyme exhibited improved bioelectrochemical behaviour, with enhanced anodic currents compared to the native enzyme. Marcus theory-based theoretical calculations revealed that hole hopping through the internal residues and from the electrode to the bioconjugated residues of the enzyme is thermodynamically favourable. The rate-limiting step for the bioelectrocatalytic process was identified as hole injection from the electrode to the bioconjugated enzyme surface. These findings demonstrate the potential of bioconjugated glucose oxidase for single molecule-based biosensing and bioelectronics.
ER  -

VECELYTE, Guoda; Vygaile DUDKAITE; Ondrej ŠEDO; Zbyněk ZDRÁHAL a Gintautas BAGDZIUNAS. Tyrosine-specific bioconjugation allowing hole hopping along aromatic chains of glucose oxidase. \textit{Materials Horizons}. Royal Society of Chemistry, 2025, roč.~12, č.~16, s.~6301-6309. ISSN~2051-6347. Dostupné z: https://doi.org/10.1039/d5mh00520e.

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