Issue 45, 2022

Multiple electron transfer pathways of tungsten-containing formate dehydrogenase in direct electron transfer-type bioelectrocatalysis

Abstract

Tungsten-containing formate dehydrogenase from Methylorubrum extroquens AM1 (FoDH1)—a promising biocatalyst for the interconversion of carbon dioxide/formate and nicotine adenine dinucleotide (NAD+)/NADH redox couples—was investigated using structural biology and bioelectrochemistry. FoDH1 is reported to be an enzyme that can realize “direct electron transfer (DET)-type bioelectrocatalysis.” However, its 3-D structure, electrode-active sites, and electron transfer (ET) pathways remain unclear. The ET pathways were investigated using structural information, electrostatic interactions between the electrode and the enzyme, and the differences in the substrates. Two electrode-active sites and multiple ET pathways in FoDH1 were discovered.

Graphical abstract: Multiple electron transfer pathways of tungsten-containing formate dehydrogenase in direct electron transfer-type bioelectrocatalysis

Supplementary files

Article information

Article type
Communication
Submitted
17 mars 2022
Accepted
27 avr. 2022
First published
29 avr. 2022

Chem. Commun., 2022,58, 6478-6481

Multiple electron transfer pathways of tungsten-containing formate dehydrogenase in direct electron transfer-type bioelectrocatalysis

T. Yoshikawa, F. Makino, T. Miyata, Y. Suzuki, H. Tanaka, K. Namba, K. Kano, K. Sowa, Y. Kitazumi and O. Shirai, Chem. Commun., 2022, 58, 6478 DOI: 10.1039/D2CC01541B

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements