ePrints

Formate hydrogenlyase, formic acid translocation and hydrogen production: dynamic membrane biology during fermentation

Lookup NU author(s): Professor Frank SargentORCiD

Downloads

• Published version [.pdf]

Licence

This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).

Abstract

© 2022. Formate hydrogenlyase-1 (FHL-1) is a complex-I-like enzyme that is commonly found in gram-negative bacteria. The enzyme comprises a peripheral arm and a membrane arm but is not involved in quinone reduction. Instead, FHL-1 couples formate oxidation to the reduction of protons to molecular hydrogen (H2). Escherichia coli produces FHL-1 under fermentative conditions where it serves to detoxify formic acid in the environment. The membrane biology and bioenergetics surrounding E. coli FHL-1 have long held fascination. Here, we review recent work on understanding the molecular basis of formic acid efflux and influx. We also consider the structure and function of E. coli FHL-1, its relationship with formate transport, and pay particular attention to the molecular interface between the peripheral arm and the membrane arm. Finally, we highlight the interesting phenotype of genetic mutation of the ND1 Loop, which is located at that interface.

Publication metadata

Author(s): Peters K, Sargent F

Publication type: Article

Publication status: Published

Journal: Biochimica et Biophysica Acta - Bioenergetics

Year: 2023

Volume: 1864

Issue: 1

Print publication date: 01/01/2023

Online publication date: 21/09/2022

Acceptance date: 19/09/2022

Date deposited: 13/10/2022

ISSN (print): 0005-2728

ISSN (electronic): 1879-2650

Publisher: Elsevier BV

URL: https://doi.org/10.1016/j.bbabio.2022.148919

DOI: 10.1016/j.bbabio.2022.148919

Altmetrics

Funding

Share