Electron spin resonance studies on a flavoprotein in neutrophil plasma membranes. Redox potentials of the flavin and its participation in NADPH oxidase.
Open accessAbstract
Plasma membrane fractions of stimulated and resting cells were isolated from pig blood neutrophils. The midpoint redox potential (Em) of the membrane-bound flavin was determined potentiometrically by analysis of the flavin free-radical signal by electron spin resonance (ESR) spectroscopy. In both stimulated and resting cells, a peak position of the titration curve gave an Em value of -280 mV at pH 7.0 (Em7). The flavin free radical showed an ESR spectrum at g = 2.004 with a peak to peak width of 19 G, which indicates that the redox intermediate is a neutral semiquinone. Redox titrations were anaerobically examined at 25 degrees C with NADPH in place of dithionite. Addition of NADPH to plasma membranes of stimulated cells resulted in a rapid change in potential, accompanied by the formation of the ESR signal of flavin free radical. Computer simulation of the titration points gave an ambient midpoint potential of -280 mV (Em7). In contrast, those of resting cells showed a very slow change in potential and no g = 2.00 signal formation. Power saturation behavior of the ESR signal showed a marked difference between those of stimulated and resting cells. ESR characteristics of the flavin are discussed in relation to the membrane-bound NADPH oxidase.
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The flavoprotein domain binds the cofactor FAD and includes a binding site for NADPH.
“The transmembrane domain includes four conserved histidines that serve as binding sites for two heme moieties bound between helices III and V (288, 613), and the flavoprotein domain binds the cofactor FAD and includes a binding site for NADPH (49, 480, 613, 980).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [480]
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- Authors
- Kakinuma, K., Kaneda, M., Chiba, T., & Ohnishi, T.
- Affiliations
- University of Tsukuba (JP)
- ORCID
- Chiba, T
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1986-07
- Volume
- 261
- Issue
- 20
- Pages
- 9426-9432
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1606670757
- Cited by
- 90
- References
- 34
- Citations by year
- 2023: 3 · 2018: 2 · 2014: 2 · 2013: 1 · 2012: 3
- FWCI
- 3.58
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Toxicology › Bioactive Compounds and Antitumor Agents
- Keywords
- flavoprotein, flavin redox potential, NADPH oxidase, flavin semiquinone, neutrophil activation, redox titration, power saturation
- MeSH terms
- Animals, Cell Membrane, Electron Spin Resonance Spectroscopy, Electron Transport, Flavoproteins, Free Radicals, Hydrogen-Ion Concentration, NADH, NADPH Oxidoreductases, NADP, Neutrophils, Oxidation-Reduction, Potentiometry, Swine, Thermodynamics, NADPH Oxidases
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