Electrochemical characterization of mutant forms of rubredoxin B from Mycobacterium tuberculosis.

Amphiphilic diblock copolymer Carbon nanotubes Cytochrome P450 Electroanalysis Mycobacterium tuberculosis Rubredoxins Screen-printed electrodes electron transfer

Journal

Biochimica et biophysica acta. Proteins and proteomics
ISSN: 1878-1454
Titre abrégé: Biochim Biophys Acta Proteins Proteom
Pays: Netherlands
ID NLM: 101731734

Informations de publication

Date de publication:
01 2022
Historique:
received: 02 07 2021
revised: 09 09 2021
accepted: 12 10 2021
pubmed: 19 10 2021
medline: 30 12 2021
entrez: 18 10 2021
Statut: ppublish

Résumé

Electron transfer in metalloproteins is a driving force for many biological processes and widely distributed in nature. Rubredoxin B (RubB) from Mycobacterium tuberculosis is a first example among [1Fe-0S] proteins that support catalytic activity of terminal sterol-monooxygenases enabling its application in metabolic engineering. To explore the tolerance of RubB to the specific amino acid changes we evaluated the effect of surface mutations on its electrochemical properties. Based on the RubB fold we also designed the mutant with a putative additional site for protein-protein interactions to further evaluate electron transfer and electrochemical properties. The investigation of redox properties of mutant variants of RubB was done using screen-printed graphite electrodes (SPEs) modified with stable dispersion of multi-walled carbon nanotubes (MWCNTs). The redox potentials (midpoint potentials, E

Identifiants

pubmed: 34662730
pii: S1570-9639(21)00140-0
doi: 10.1016/j.bbapap.2021.140734
pii:
doi:

Substances chimiques

Rubredoxins 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

140734

Informations de copyright

Copyright © 2021. Published by Elsevier B.V.

Auteurs

Andrei Gilep (A)

Institute of Bioorganic Chemistry, National Academy of Sciences of Belarus, Minsk, Belarus; Institute of Biomedical Chemistry, Moscow, Russia.

Alexey Kuzikov (A)

Institute of Biomedical Chemistry, Moscow, Russia; Pirogov Russian National Research Medical University, Moscow, Russia.

Tatsiana Sushko (T)

IMSUT, The University of Tokyo, Tokyo, Japan.

Irina Grabovec (I)

Institute of Bioorganic Chemistry, National Academy of Sciences of Belarus, Minsk, Belarus.

Rami Masamrekh (R)

Institute of Biomedical Chemistry, Moscow, Russia; Pirogov Russian National Research Medical University, Moscow, Russia.

Larisa V Sigolaeva (LV)

Department of Chemistry, M.V. Lomonosov Moscow State University, 119991 Moscow, Russia.

Dmitry V Pergushov (DV)

Department of Chemistry, M.V. Lomonosov Moscow State University, 119991 Moscow, Russia.

Felix H Schacher (FH)

Institute of Organic Chemistry and Macromolecular Chemistry (IOMC), Friedrich-Schiller-University Jena, D-07743 Jena, Germany; Jena Center for Soft Matter (JCSM), Friedrich-Schiller-University Jena, D-07743 Jena, Germany; Center for Energy and Environmental Chemistry (CEEC), Friedrich-Schiller-University Jena, D-07743 Jena, Germany.

Natallia Strushkevich (N)

Skolkovo Institute of Science and Technology, Moscow, Russia. Electronic address: n.strushkevich@skoltech.ru.

Victoria V Shumyantseva (VV)

Institute of Biomedical Chemistry, Moscow, Russia; Pirogov Russian National Research Medical University, Moscow, Russia. Electronic address: viktoria.shumyantseva@ibmc.msk.ru.

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