ArticleProceedings of the National Academy of Sciences of the United States of America2017
Unprecedented pathway of reducing equivalents in a diflavin-linked disulfide oxidoreductase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 12 citations in OpenAlex.
- Exploring the Diversity of the Thioredoxin Systems in Cyanobacteria.Antioxidants (Basel, Switzerland) · 2022Review
- Depletion of m-type thioredoxin impairs photosynthesis, carbon fixation, and oxidative stress in cyanobacteria.Plant physiology · 2021Article
- Atomic Force Microscopy to Elicit Conformational Transitions of Ferredoxin-Dependent Flavin Thioredoxin Reductases.Antioxidants (Basel, Switzerland) · 2021Article
- Metal(loid) speciation and transformation by aerobic methanotrophs.Microbiome · 2021Review
- Unexpected diversity of ferredoxin-dependent thioredoxin reductases in cyanobacteria.Plant physiology · 2021Article
- Emissive Enhancement of the Singlet Oxygen Chemiluminescence Probe after Binding to Bovine Serum Albumin.Molecules (Basel, Switzerland) · 2019Article
- A Novel Clinical Six-Flavoprotein-Gene Signature Predicts Prognosis in Esophageal Squamous Cell Carcinoma.BioMed research international · 2019Article
- Characterization of TrxC, an Atypical Thioredoxin Exclusively Present in Cyanobacteria.Antioxidants (Basel, Switzerland) · 2018Article
Corrections and comments
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Authors and funding
11 authors at 8 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Flavoproteins participate in a wide variety of physiologically relevant processes that typically involve redox reactions. Within this protein superfamily, there exists a group that is able to transfer reducing equivalents from FAD to a redox-active disulfide bridge, which further reduces disulfide bridges in target proteins to regulate their structure and function. We have identified a previously undescribed type of flavin enzyme that is exclusive to oxygenic photosynthetic prokaryotes and that is based on the primary sequence that had been assigned as an NADPH-dependent thioredoxin reductase (NTR). However, our experimental data show that the protein does not transfer reducing equivalents from flavins to disulfides as in NTRs but functions in the opposite direction. High-resolution structures of the protein from
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