ArticleThe Journal of biological chemistry2015
The extracellular A-loop of dual oxidases affects the specificity of reactive oxygen species release.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 38 citations in OpenAlex.
- Expression, localization and regulation of NADPH oxidases in pancreatic beta cells.Redox report : communications in free radical research · 2025Article
- Bioluminescence-Based Complementation Assay to Correlate Conformational Changes in Membrane-Bound Complexes with Enzymatic Function.Methods in molecular biology (Clifton, N.J.) · 2022Article
- The TGF-β/NADPH Oxidases Axis in the Regulation of Liver Cell Biology in Health and Disease.Cells · 2021Review
- Deploying new generation sequencing for the study of flesh color depletion in Atlantic Salmon (Salmo salar).BMC genomics · 2021Article
- DUOX1 in mammalian disease pathophysiology.Journal of molecular medicine (Berlin, Germany) · 2021Review
- NADPH Oxidases (NOX): An Overview from Discovery, Molecular Mechanisms to Physiology and Pathology.Antioxidants (Basel, Switzerland) · 2021Review
- Structures of human dual oxidase 1 complex in low-calcium and high-calcium states.Nature communications · 2021Article
- The genetic structure and adaptation of Andean highlanders and Amazonians are influenced by the interplay between geography and culture.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Structures of mouse DUOX1-DUOXA1 provide mechanistic insights into enzyme activation and regulation.Nature structural & molecular biology · 2020Article
- Pharmacological characterization of the seven human NOX isoforms and their inhibitors.Redox biology · 2019Article
- Review
- Antimicrobial actions of dual oxidases and lactoperoxidase.Journal of microbiology (Seoul, Korea) · 2018Review
- Autophagy regulates DUOX1 localization and superoxide production in airway epithelial cells during chronic IL-13 stimulation.Redox biology · 2018Article
- Paradoxical roles of dual oxidases in cancer biology.Free radical biology & medicine · 2017Review
- Nox5 stability and superoxide production is regulated by C-terminal binding of Hsp90 and CO-chaperones.Free radical biology & medicine · 2015Article
- Genetic disorders coupled to ROS deficiency.Redox biology · 2015Review
- Enzymatic regulation and functional relevance of NOX5.Current pharmaceutical design · 2015Review
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 4 countries.
Funding
Abstract
NADPH oxidase (Nox) family proteins produce superoxide (O2 (⨪)) directly by transferring an electron to molecular oxygen. Dual oxidases (Duoxes) also produce an O2 (⨪) intermediate, although the final species secreted by mature Duoxes is H2O2, suggesting that intramolecular O2 (⨪) dismutation or other mechanisms contribute to H2O2 release. We explored the structural determinants affecting reactive oxygen species formation by Duox enzymes. Duox2 showed O2 (⨪) leakage when mismatched with Duox activator 1 (DuoxA1). Duox2 released O2 (⨪) even in correctly matched combinations, including Duox2 + DuoxA2 and Duox2 + N-terminally tagged DuoxA2 regardless of the type or number of tags. Conversely, Duox1 did not release O2 (⨪) in any combination. Chimeric Duox2 possessing the A-loop of Duox1 showed no O2 (⨪) leakage; chimeric Duox1 possessing the A-loop of Duox2 released O2 (⨪). Moreover, Duox2 proteins possessing the A-loops of Nox1 or Nox5 co-expressed with DuoxA2 showed enhanced O2 (⨪) release, and Duox1 proteins possessing the A-loops of Nox1 or Nox5 co-expressed with DuoxA1 acquired O2 (⨪) leakage. Although we identified Duox1 A-loop residues (His(1071), His(1072), and Gly(1074)) important for reducing O2 (⨪) release, mutations of these residues to those of Duox2 failed to convert Duox1 to an O2 (⨪)-releasing enzyme. Using immunoprecipitation and endoglycosidase H sensitivity assays, we found that the A-loop of Duoxes binds to DuoxA N termini, creating more stable, mature Duox-DuoxA complexes. In conclusion, the A-loops of both Duoxes support H2O2 production through interaction with corresponding activators, but complex formation between the Duox1 A-loop and DuoxA1 results in tighter control of H2O2 release by the enzyme complex.
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