Superoxide-forming enzyme from human neutrophils: Evidence for a flavin requirement

Babior, BM; Kipnes, RS

doi:10.1182/blood.v50.3.517.517

Cited by 174Neutrophil, Myeloperoxidase and Oxidative MechanismsRedox biology and oxidative stressBioactive Compounds and Antitumor Agents

Superoxide-forming enzyme from human neutrophils: Evidence for a flavin requirement

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Babior, BM, Kipnes, RS·1977·Blood

DOI 10.1182/blood.v50.3.517.517

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Abstract

The superoxide-forming activity of 27,000-g particles prepared from homogenates of zymosan-treated human neutrophils is lost if the assay is conducted in the presence of 0.045% Triton X-100. This loss in activity in the presence of detergent is prevented by 40 micron flavin adenine dinucleotide (FAD), but not by flavin mononucleotide, riboflavin, adenosine 5′-diphosphate, or adenosine 5′-monophosphate. With resting particles or particles from zymosan-treated chronic granulomatous disease neutrophils, no superoxide-forming activity is detectable even in the presence of FAD; this is true whether or not detergent is present in the assay. Particles extracted with detergent prior to assay are fully active if assayed in the presence of FAD, but show little activity if FAD is omitted from the assay mixture. These results suggest that the superoxide-forming enzyme from human neutrophils is a FAD-requiring enzyme.

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NOX2 is predominantly expressed in phagocytes and produces a relatively large amount of superoxide in order to kill bacteria within phagosomes in an inflamed area.
“NOX2 is predominantly expressed in phagocytes and produces a relatively large amount of superoxide in order to kill bacteria within phagosomes in an inflamed area [33,34], Figure 13.”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [33]
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 [49]

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Authors: Babior, B., & Kipnes, R.
Venue: Blood
Publisher: American Society of Hematology
Published: 1977-09-01
Volume: 50
Issue: 3
Pages: 517-524
ISSN: 0006-4971 (ISSN-L)
1528-0020
DOI: 10.1182/blood.v50.3.517.517
OpenAlex: W2475048516
Cited by: 174
References: 23
Citations by year: 2023: 4 · 2022: 2 · 2021: 2 · 2019: 3 · 2018: 1 · 2016: 1 · 2014: 2 · 2013: 1
FWCI: 2.86
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Blood (publishedVersion)
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: neutrophils, flavin adenine dinucleotide, NADPH oxidase, zymosan, chronic granulomatous disease, detergent extraction, Triton X-100, flavin mononucleotide, riboflavin
MeSH terms: Adenine Nucleotides, Detergents, Flavins, Granulomatous Disease, Chronic, Humans, Neutrophils, Peroxides, Zymosan

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Superoxide-forming enzyme from human neutrophils: Evidence for a flavin requirement

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