Constitutive NADPH-Dependent Electron Transferase Activity of the Nox4 Dehydrogenase Domain
Open accessAbstract
NADPH oxidase 4 (Nox4) is constitutively active, while Nox2 requires the cytosolic regulatory subunits p47(phox) and p67(phox) and activated Rac with activation by phorbol 12-myristate 13-acetate (PMA). This study was undertaken to identify the domain on Nox4 that confers constitutive activity. Lysates from Nox4-expressing cells exhibited constitutive NADPH- but not NADH-dependent hydrogen peroxide production with a K(m) for NADPH of 55 +/- 10 microM. The concentration of Nox4 in cell lysates was estimated using Western blotting and allowed calculation of a turnover of approximately 200 mol of H(2)O(2) min(-1) (mol of Nox4)(-1). A chimeric protein (Nox2/4) consisting of the Nox2 transmembrane (TM) domain and the Nox4 dehydrogenase (DH) domain showed H(2)O(2) production in the absence of cytosolic regulatory subunits. In contrast, chimera Nox4/2, consisting of the Nox4 TM and Nox2 DH domains, exhibited PMA-dependent activation that required coexpression of regulatory subunits. Nox DH domains from several Nox isoforms were purified and evaluated for their electron transferase activities. Nox1 DH, Nox2 DH, and Nox5 DH domains exhibited barely detectable activities toward artificial electron acceptors, while the Nox4 DH domain exhibited significant rates of reduction of cytochrome c (160 min(-1), largely superoxide dismutase-independent), ferricyanide (470 min(-1)), and other electron acceptors (artificial dyes and cytochrome b(5)). Rates were similar to those observed for H(2)O(2) production by the Nox4 holoenzyme in cell lysates. The activity required added FAD and was seen with NADPH but not NADH. These results indicate that the Nox4 DH domain exists in an intrinsically activated state and that electron transfer from NADPH to FAD is likely to be rate-limiting in the NADPH-dependent reduction of oxygen by holo-Nox4.
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Oxidation of cysteine residues 535 and 992 in rat or bovine XDH or limited proteolysis turns XDH into XO.
“Oxidation of cysteine residues 535 and 992 in rat or bovine XDH or limited proteolysis turns XDH into XO (23, 72, 693, 773, 803, 994).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [693]
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- Authors
- Nisimoto, Y., Jackson, H. M., Ogawa, H., Kawahara, T., & Lambeth, J. D.
- Affiliations
- Emory University (US)
- Fujita Health University (JP)
- Corresponding author
- Lambeth, J. David
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2010-02-25
- Volume
- 49
- Issue
- 11
- Pages
- 2433-2442
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- PMC
- PMC2839512
- OpenAlex
- W2074985423
- Cited by
- 161
- References
- 59
- Citations by year
- 2026: 6 · 2025: 5 · 2024: 14 · 2023: 11 · 2022: 6 · 2021: 8 · 2020: 9 · 2019: 6 · 2018: 6 · 2017: 12 · 2016: 7 · 2015: 11 · 2014: 12 · 2013: 17 · 2012: 12
- FWCI
- 6.25
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Biochemistry (publishedVersion, other-oa)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- American Heart Association
- Emory University
- National Institutes of Health (CA105116)
- National Cancer Institute (CA 105116)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Keywords
- NOX4, NADPH oxidase, FAD, hydrogen peroxide production, cytochrome c reduction, ferricyanide reduction, cytochrome b5, NOX2, NOX1, NADPH oxidase 5, fusion protein, p47phox, p67phox, Rac activation, phorbol myristate acetate
- MeSH terms
- NADPH Oxidase 2, NADPH Oxidase 4, Cell Extracts, Cell Line, Cell Membrane, Cytosol, Electron Transport, Flavin-Adenine Dinucleotide, Humans, Kinetics, Membrane Glycoproteins, NADP, Oxidoreductases, Solubility, Substrate Specificity, Transferases, Reactive Oxygen Species, Sequence Homology, Amino Acid, Protein Structure, Tertiary, Protein Folding, NADPH Oxidases, Holoenzymes, Protein Transport
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