ArticleProtein science : a publication of the Protein Society2025
An iron-sulfur cluster as a new metal center in a flavodiiron protein.
Article in Protein science : a publication of the Protein Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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.
The trial behind it
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Who cites it
2 citing papers in PubMed.
- Structures of variants of Escherichia coli flavodiiron-type nitric oxide reductase reveal changes in the di-iron site.Acta crystallographica. Section D, Structural biology · 2026Article
- An iron-sulfur cluster as a new metal center in a flavodiiron protein.Protein science : a publication of the Protein Society · 2025Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Syntrophomonas wolfei contains two distinct multiple domain flavodiiron proteins (FDPs) of Classes H and E, presumably acting as oxygen reductases to protect this anaerobic bacterium from oxidative stress due to exposure to environments containing, even if only transiently, oxygen. The Class E FDP was previously predicted by us to have, besides the two core domains characteristic of this type of enzymes, an extra C-terminal domain putatively harboring an iron-sulfur center. This C-terminal domain is exclusive to this class of FDPs and has homology with a protein domain family "Fer4_19" which may contain a [3Fe-4S]
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Registered trials
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