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| CYTOCHROME-B558 - THE FLAVIN-BINDING COMPONENT OF THE PHAGOCYTE NADPH OXIDASE |
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| Author(s): ROTROSEN D, YEUNG CL, LETO TL, MALECH HL, KWONG CH |
| Source: SCIENCE Volume: 256 Issue: 5062 Pages: 1459-1462 Published: JUN 5 1992 |
| Times Cited: 322 References: 48 |
| Abstract: The phagocyte respiratory burst oxidase is a flavin-adenine dinucleotide (FAD)-dependent dehydrogenase and an electron transferase that reduces molecular oxygen to superoxide anion, a precursor of microbicidal oxidants. Several proteins required for assembly of the oxidase have been characterized, but the identity of its flavin-binding component has been unclear. Oxidase activity was reconstituted in vitro with only the purified oxidase proteins p47phox, p67phox, Rac-related guanine nucleotide (GTP)-binding proteins, and membrane-bound cytochrome b558. The reconstituted oxidase required added FAD, and FAD binding was localized to cytochrome b558. Alignment of the amino acid sequence of the beta-subunit of cytochrome b558 (gp91phox) with other flavoproteins revealed similarities to the nicotinamide adenine dinucleotide phosphate (reduced) (NADPH)-binding domains. Thus flavocytochrome b558 is the only obligate electron transporting component of the NADPH oxidase. |
| Document Type: Article |
| Language: English |
| Reprint Address: ROTROSEN, D (reprint author), NIAID, HOST DEF LAB, BETHESDA, MD 20892 USA |
| Publisher: AMER ASSOC ADVANCEMENT SCIENCE, 1200 NEW YORK AVE, NW, WASHINGTON, DC 20005 |
| Subject Category: Multidisciplinary Sciences |
| IDS Number: HX337 |
| ISSN: 0036-8075 |
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