Changing the Tracks: Screening for Electron Transfer Proteins to Support Hydrogen Production

Overview

Journal J Biol Inorg Chem

Publisher Springer

Specialty Biochemistry

Date 2022 Aug 29

PMID 36038787

Authors

Alexander Gunzel

Vera Engelbrecht

Thomas Happe

Affiliations

Soon will be listed here.

Abstract

Ferredoxins are essential electron transferring proteins in organisms. Twelve plant-type ferredoxins in the green alga Chlamydomonas reinhardtii determine the fate of electrons, generated in multiple metabolic processes. The two hydrogenases HydA1 and HydA2 of. C. reinhardtii compete for electrons from the photosynthetic ferredoxin PetF, which is the first stromal mediator of the high-energy electrons derived from the absorption of light energy at the photosystems. While being involved in many chloroplast-located metabolic pathways, PetF shows the highest affinity for ferredoxin-NADP oxidoreductase (FNR), not for the hydrogenases. Aiming to identify other potential electron donors for the hydrogenases, we screened as yet uncharacterized ferredoxins Fdx7, 8, 10 and 11 for their capability to reduce the hydrogenases. Comparing the performance of the Fdx in presence and absence of competitor FNR, we show that Fdx7 has a higher affinity for HydA1 than for FNR. Additionally, we show that synthetic FeS-cluster-binding maquettes, which can be reduced by NADPH alone, can also be used to reduce the hydrogenases. Our findings pave the way for the creation of tailored electron donors to redirect electrons to enzymes of interest.

Citing Articles

The Alga Has Two Structural Types of [FeFe]-Hydrogenases with Different Biochemical Properties.

Alavi G, Engelbrecht V, Hemschemeier A, Happe T Int J Mol Sci. 2023; 24(24).

PMID: 38139142 PMC: 10744039. DOI: 10.3390/ijms242417311.

Novel concepts and engineering strategies for heterologous expression of efficient hydrogenases in photosynthetic microorganisms.

Schumann C, Fernandez Mendez J, Berggren G, Lindblad P Front Microbiol. 2023; 14:1179607.

PMID: 37502399 PMC: 10369191. DOI: 10.3389/fmicb.2023.1179607.

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