Standard

Solid-State Nanopore-Based Nanosystem for Registration of Enzymatic Activity of a Single Molecule of Cytochrome P450 BM3. / Ivanov, Y.D.; Vinogradova, A.V.; Nevedrova, E.D.; Ableev, A.N.; Kozlov, A.F.; Shumov, I.D.; Ziborov, V.S.; Afonin, O.N.; Vaulin, N.V.; Lebedev, D.V.; Bukatin, A.S.; Afonicheva, P.K.; Mukhin, I.S.; Usanov, S.A.; Archakov, A.I.

в: International Journal of Molecular Sciences, Том 25, № 19, 09.10.2024.

Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование

Harvard

Ivanov, YD, Vinogradova, AV, Nevedrova, ED, Ableev, AN, Kozlov, AF, Shumov, ID, Ziborov, VS, Afonin, ON, Vaulin, NV, Lebedev, DV, Bukatin, AS, Afonicheva, PK, Mukhin, IS, Usanov, SA & Archakov, AI 2024, 'Solid-State Nanopore-Based Nanosystem for Registration of Enzymatic Activity of a Single Molecule of Cytochrome P450 BM3', International Journal of Molecular Sciences, Том. 25, № 19. https://doi.org/10.3390/ijms251910864

APA

Ivanov, Y. D., Vinogradova, A. V., Nevedrova, E. D., Ableev, A. N., Kozlov, A. F., Shumov, I. D., Ziborov, V. S., Afonin, O. N., Vaulin, N. V., Lebedev, D. V., Bukatin, A. S., Afonicheva, P. K., Mukhin, I. S., Usanov, S. A., & Archakov, A. I. (2024). Solid-State Nanopore-Based Nanosystem for Registration of Enzymatic Activity of a Single Molecule of Cytochrome P450 BM3. International Journal of Molecular Sciences, 25(19). https://doi.org/10.3390/ijms251910864

Vancouver

Ivanov YD, Vinogradova AV, Nevedrova ED, Ableev AN, Kozlov AF, Shumov ID и пр. Solid-State Nanopore-Based Nanosystem for Registration of Enzymatic Activity of a Single Molecule of Cytochrome P450 BM3. International Journal of Molecular Sciences. 2024 Окт. 9;25(19). https://doi.org/10.3390/ijms251910864

Author

Ivanov, Y.D. ; Vinogradova, A.V. ; Nevedrova, E.D. ; Ableev, A.N. ; Kozlov, A.F. ; Shumov, I.D. ; Ziborov, V.S. ; Afonin, O.N. ; Vaulin, N.V. ; Lebedev, D.V. ; Bukatin, A.S. ; Afonicheva, P.K. ; Mukhin, I.S. ; Usanov, S.A. ; Archakov, A.I. / Solid-State Nanopore-Based Nanosystem for Registration of Enzymatic Activity of a Single Molecule of Cytochrome P450 BM3. в: International Journal of Molecular Sciences. 2024 ; Том 25, № 19.

BibTeX

@article{49c4dc860c62415c951c3788580125ee,
title = "Solid-State Nanopore-Based Nanosystem for Registration of Enzymatic Activity of a Single Molecule of Cytochrome P450 BM3",
abstract = "Experimental methods of single-molecule enzymology allow scientists to determine physicochemical properties of distinct single molecules of various enzymes and to perform direct monitoring of functioning of enzymes at different steps of their catalytic cycle. The approach based on the use of solid-state nanopores is a promising tool for studying the functioning of single-enzyme molecules. Herein, this approach is employed for monitoring the functioning of cytochrome P450 BM3, which represents a very convenient model of cytochrome P450-containing monooxygenase systems. A nanopore of ~5 nm in diameter has been formed in a 40 nm-thick silicon nitride chip by electron beam drilling (EBD), and a single molecule of the BM3 enzyme has been entrapped in the pore. The functioning of the enzyme molecule has been monitored by recording the time dependence of the ion current through the nanopore during the reaction of laurate hydroxylation. In our experiments, the enzyme molecule has been found to be active for 1500 s. The results of our research can be further used in the development of highly sensitive detectors for single-molecule studies in enzymology. {\textcopyright} 2024 by the authors.",
keywords = "cytochrome P450 BM3, enzyme functioning, nanopore detector, solid-state nanopore, bacterial protein, cytochrome P450, flavocytochrome P450 BM3 monoxygenases, reduced nicotinamide adenine dinucleotide phosphate ferrihemoprotein reductase, chemistry, metabolism, nanopore, procedures, single molecule imaging, Bacterial Proteins, Cytochrome P-450 Enzyme System, NADPH-Ferrihemoprotein Reductase, Nanopores, Single Molecule Imaging, NADPH-Ferrihemoprotein Reductase/metabolism, Cytochrome P-450 Enzyme System/metabolism, Single Molecule Imaging/methods, Bacterial Proteins/chemistry",
author = "Y.D. Ivanov and A.V. Vinogradova and E.D. Nevedrova and A.N. Ableev and A.F. Kozlov and I.D. Shumov and V.S. Ziborov and O.N. Afonin and N.V. Vaulin and D.V. Lebedev and A.S. Bukatin and P.K. Afonicheva and I.S. Mukhin and S.A. Usanov and A.I. Archakov",
note = "Export Date: 27 October 2024 Химические вещества/CAS: cytochrome P450, 9035-51-2; reduced nicotinamide adenine dinucleotide phosphate ferrihemoprotein reductase, 9023-03-4; Bacterial Proteins; Cytochrome P-450 Enzyme System; flavocytochrome P450 BM3 monoxygenases; NADPH-Ferrihemoprotein Reductase Сведения о финансировании: Ministry of Education and Science of the Russian Federation, Minobrnauka, 075-15-2024-643 Текст о финансировании 1: This work was financed by the Ministry of Science and Higher Education of the Russian Federation within the framework of Agreement \u2116 075-15-2024-643.",
year = "2024",
month = oct,
day = "9",
doi = "10.3390/ijms251910864",
language = "Английский",
volume = "25",
journal = "International Journal of Molecular Sciences",
issn = "1422-0067",
publisher = "MDPI AG",
number = "19",

}

RIS

TY - JOUR

T1 - Solid-State Nanopore-Based Nanosystem for Registration of Enzymatic Activity of a Single Molecule of Cytochrome P450 BM3

AU - Ivanov, Y.D.

AU - Vinogradova, A.V.

AU - Nevedrova, E.D.

AU - Ableev, A.N.

AU - Kozlov, A.F.

AU - Shumov, I.D.

AU - Ziborov, V.S.

AU - Afonin, O.N.

AU - Vaulin, N.V.

AU - Lebedev, D.V.

AU - Bukatin, A.S.

AU - Afonicheva, P.K.

AU - Mukhin, I.S.

AU - Usanov, S.A.

AU - Archakov, A.I.

N1 - Export Date: 27 October 2024 Химические вещества/CAS: cytochrome P450, 9035-51-2; reduced nicotinamide adenine dinucleotide phosphate ferrihemoprotein reductase, 9023-03-4; Bacterial Proteins; Cytochrome P-450 Enzyme System; flavocytochrome P450 BM3 monoxygenases; NADPH-Ferrihemoprotein Reductase Сведения о финансировании: Ministry of Education and Science of the Russian Federation, Minobrnauka, 075-15-2024-643 Текст о финансировании 1: This work was financed by the Ministry of Science and Higher Education of the Russian Federation within the framework of Agreement \u2116 075-15-2024-643.

PY - 2024/10/9

Y1 - 2024/10/9

N2 - Experimental methods of single-molecule enzymology allow scientists to determine physicochemical properties of distinct single molecules of various enzymes and to perform direct monitoring of functioning of enzymes at different steps of their catalytic cycle. The approach based on the use of solid-state nanopores is a promising tool for studying the functioning of single-enzyme molecules. Herein, this approach is employed for monitoring the functioning of cytochrome P450 BM3, which represents a very convenient model of cytochrome P450-containing monooxygenase systems. A nanopore of ~5 nm in diameter has been formed in a 40 nm-thick silicon nitride chip by electron beam drilling (EBD), and a single molecule of the BM3 enzyme has been entrapped in the pore. The functioning of the enzyme molecule has been monitored by recording the time dependence of the ion current through the nanopore during the reaction of laurate hydroxylation. In our experiments, the enzyme molecule has been found to be active for 1500 s. The results of our research can be further used in the development of highly sensitive detectors for single-molecule studies in enzymology. © 2024 by the authors.

AB - Experimental methods of single-molecule enzymology allow scientists to determine physicochemical properties of distinct single molecules of various enzymes and to perform direct monitoring of functioning of enzymes at different steps of their catalytic cycle. The approach based on the use of solid-state nanopores is a promising tool for studying the functioning of single-enzyme molecules. Herein, this approach is employed for monitoring the functioning of cytochrome P450 BM3, which represents a very convenient model of cytochrome P450-containing monooxygenase systems. A nanopore of ~5 nm in diameter has been formed in a 40 nm-thick silicon nitride chip by electron beam drilling (EBD), and a single molecule of the BM3 enzyme has been entrapped in the pore. The functioning of the enzyme molecule has been monitored by recording the time dependence of the ion current through the nanopore during the reaction of laurate hydroxylation. In our experiments, the enzyme molecule has been found to be active for 1500 s. The results of our research can be further used in the development of highly sensitive detectors for single-molecule studies in enzymology. © 2024 by the authors.

KW - cytochrome P450 BM3

KW - enzyme functioning

KW - nanopore detector

KW - solid-state nanopore

KW - bacterial protein

KW - cytochrome P450

KW - flavocytochrome P450 BM3 monoxygenases

KW - reduced nicotinamide adenine dinucleotide phosphate ferrihemoprotein reductase

KW - chemistry

KW - metabolism

KW - nanopore

KW - procedures

KW - single molecule imaging

KW - Bacterial Proteins

KW - Cytochrome P-450 Enzyme System

KW - NADPH-Ferrihemoprotein Reductase

KW - Nanopores

KW - Single Molecule Imaging

KW - NADPH-Ferrihemoprotein Reductase/metabolism

KW - Cytochrome P-450 Enzyme System/metabolism

KW - Single Molecule Imaging/methods

KW - Bacterial Proteins/chemistry

UR - https://www.mendeley.com/catalogue/4d28589b-02cc-34c0-9633-c12dc276b530/

U2 - 10.3390/ijms251910864

DO - 10.3390/ijms251910864

M3 - статья

C2 - 39409193

VL - 25

JO - International Journal of Molecular Sciences

JF - International Journal of Molecular Sciences

SN - 1422-0067

IS - 19

ER -

ID: 126461555