ArticleFEBS letters2017
Identification of a stable complex between a [NiFe]-hydrogenase catalytic subunit and its maturation protease.
Article in FEBS letters, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 5 citations in OpenAlex.
- Activation of a [NiFe]-hydrogenase-4 isoenzyme by maturation proteases.Microbiology (Reading, England) · 2020Article
- A membrane-bound [NiFe]-hydrogenase large subunit precursor whose C-terminal extension is not essential for cofactor incorporation but guarantees optimal maturation.MicrobiologyOpen · 2020Article
- Molecular Hydrogen Metabolism: a Widespread Trait of Pathogenic Bacteria and Protists.Microbiology and molecular biology reviews : MMBR · 2020Review
- Delimiting the Function of the C-Terminal Extension of theFrontiers in microbiology · 2019Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Salmonella enterica serovar Typhimurium has the ability to use molecular hydrogen as a respiratory electron donor. This is facilitated by three [NiFe]-hydrogenases termed Hyd-1, Hyd-2, and Hyd-5. Hyd-1 and Hyd-5 are homologous oxygen-tolerant [NiFe]-hydrogenases. A critical step in the biosynthesis of a [NiFe]-hydrogenase is the proteolytic processing of the catalytic subunit. In this work, the role of the maturation protease encoded within the Hyd-5 operon, HydD, was found to be partially complemented by the maturation protease encoded in the Hyd-1 operon, HyaD. In addition, both maturation proteases were shown to form stable complexes, in vivo and in vitro, with the catalytic subunit of Hyd-5. The protein-protein interactions were not detectable in a strain that could not make the enzyme metallocofactor.
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