The superoxide-generating NADPH oxidase: structural aspects and activation mechanism
Flavocytochrome b558 is the catalytic core of the respiratory-burst oxidase, an enzyme complex that catalyzes the NADPH-dependent reduction of O2 into the superoxide anion O2 in phagocytic cells. Flavocytochrome b558 is anchored in the plasma membrane. It is a heterodimer that consists of a large gl...
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| description | Flavocytochrome b558 is the catalytic core of the respiratory-burst oxidase, an enzyme complex that catalyzes the NADPH-dependent reduction of O2 into the superoxide anion O2 in phagocytic cells. Flavocytochrome b558 is anchored in the plasma membrane. It is a heterodimer that consists of a large glycoprotein gp91phox (phox forphagocyte oxidase) (beta subunit) and a small protein p22phox (alpha subunit). The other components of the respiratory-burst oxidase are water-soluble proteins of cytosolic origin, namely p67phox, p47phox, p40phox and Rac. Upon cell stimulation, they assemble with the membrane-bound flavocytochrome b558 which becomes activated and generates O2-. A defect in any of the genes encoding gp91phox, p22phox, p67phox or p47phox results in chronic granulomatous disease, a genetic disorder characterized by severe and recurrent infections, illustrating the role of O2- and the derived metabolites H2O2 and HOCl in host defense against invading microorganisms. The electron carriers, FAD and hemes b, and the binding site for NADPH are confined to the gp91phox subunit of flavocytochrome b558. The p22phox subunit serves as a docking site for the cytoso lic phox proteins. This review provides an overview of current knowledge on the structural organization of the O2(-)-generating flavocytochrome b558, its kinetics, its mechanism of activation and the regulation of its biosynthesis. Homologues of gp91phox, called Nox and Duox, are present in a large variety of non-phagocytic cells. They exhibit modest O2(-)-generating oxidase activity, and some act as proton channels. Their role in various aspects of signal transduction is currently under investigation and is briefly discussed. |
| doi_str_mv | 10.1007/s00018-002-8520-9 |
| format | Article |
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Flavocytochrome b558 is anchored in the plasma membrane. It is a heterodimer that consists of a large glycoprotein gp91phox (phox forphagocyte oxidase) (beta subunit) and a small protein p22phox (alpha subunit). The other components of the respiratory-burst oxidase are water-soluble proteins of cytosolic origin, namely p67phox, p47phox, p40phox and Rac. Upon cell stimulation, they assemble with the membrane-bound flavocytochrome b558 which becomes activated and generates O2-. A defect in any of the genes encoding gp91phox, p22phox, p67phox or p47phox results in chronic granulomatous disease, a genetic disorder characterized by severe and recurrent infections, illustrating the role of O2- and the derived metabolites H2O2 and HOCl in host defense against invading microorganisms. The electron carriers, FAD and hemes b, and the binding site for NADPH are confined to the gp91phox subunit of flavocytochrome b558. The p22phox subunit serves as a docking site for the cytoso lic phox proteins. This review provides an overview of current knowledge on the structural organization of the O2(-)-generating flavocytochrome b558, its kinetics, its mechanism of activation and the regulation of its biosynthesis. Homologues of gp91phox, called Nox and Duox, are present in a large variety of non-phagocytic cells. They exhibit modest O2(-)-generating oxidase activity, and some act as proton channels. Their role in various aspects of signal transduction is currently under investigation and is briefly discussed.</description><identifier>ISSN: 1420-682X</identifier><identifier>EISSN: 1420-9071</identifier><identifier>DOI: 10.1007/s00018-002-8520-9</identifier><identifier>PMID: 12440767</identifier><language>eng</language><publisher>Switzerland: Springer Nature B.V</publisher><subject>Amino Acid Sequence ; Animals ; Binding Sites ; Biosynthesis ; Cellular biology ; Cytochrome b Group - chemistry ; Cytochrome b Group - genetics ; Cytochrome b Group - metabolism ; Electron Transport - physiology ; Enzyme Activation ; Enzymes ; Genetic disorders ; glycoproteins ; Humans ; Metabolites ; Microorganisms ; Molecular biology ; Molecular Sequence Data ; NAD(P)H oxidase (H2O2-forming) ; NADPH Oxidases - chemistry ; NADPH Oxidases - genetics ; NADPH Oxidases - metabolism ; Neutrophils - enzymology ; phagocytes ; Phosphoproteins - genetics ; Phosphoproteins - metabolism ; plasma membrane ; Protein Processing, Post-Translational ; Protein Structure, Secondary ; Protein Subunits ; Proteins ; rac GTP-Binding Proteins - metabolism ; rap1 GTP-Binding Proteins - metabolism ; respiratory burst ; signal transduction ; Structure-Activity Relationship ; superoxide anion ; Superoxides - metabolism ; water solubility</subject><ispartof>Cellular and molecular life sciences : CMLS, 2002-10, Vol.59 (9), p.1428-1459</ispartof><rights>Birkhäuser Verlag 2002</rights><rights>Birkhäuser Verlag, 2002 2002</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c570t-7fe981cb1663f19497a777a13a69f6264ff8e131a6770f7f8e10376f80809cd13</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC11337443/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC11337443/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12440767$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Vignais, P V</creatorcontrib><title>The superoxide-generating NADPH oxidase: structural aspects and activation mechanism</title><title>Cellular and molecular life sciences : CMLS</title><addtitle>Cell Mol Life Sci</addtitle><description>Flavocytochrome b558 is the catalytic core of the respiratory-burst oxidase, an enzyme complex that catalyzes the NADPH-dependent reduction of O2 into the superoxide anion O2 in phagocytic cells. Flavocytochrome b558 is anchored in the plasma membrane. It is a heterodimer that consists of a large glycoprotein gp91phox (phox forphagocyte oxidase) (beta subunit) and a small protein p22phox (alpha subunit). The other components of the respiratory-burst oxidase are water-soluble proteins of cytosolic origin, namely p67phox, p47phox, p40phox and Rac. Upon cell stimulation, they assemble with the membrane-bound flavocytochrome b558 which becomes activated and generates O2-. A defect in any of the genes encoding gp91phox, p22phox, p67phox or p47phox results in chronic granulomatous disease, a genetic disorder characterized by severe and recurrent infections, illustrating the role of O2- and the derived metabolites H2O2 and HOCl in host defense against invading microorganisms. The electron carriers, FAD and hemes b, and the binding site for NADPH are confined to the gp91phox subunit of flavocytochrome b558. The p22phox subunit serves as a docking site for the cytoso lic phox proteins. This review provides an overview of current knowledge on the structural organization of the O2(-)-generating flavocytochrome b558, its kinetics, its mechanism of activation and the regulation of its biosynthesis. Homologues of gp91phox, called Nox and Duox, are present in a large variety of non-phagocytic cells. They exhibit modest O2(-)-generating oxidase activity, and some act as proton channels. Their role in various aspects of signal transduction is currently under investigation and is briefly discussed.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Binding Sites</subject><subject>Biosynthesis</subject><subject>Cellular biology</subject><subject>Cytochrome b Group - chemistry</subject><subject>Cytochrome b Group - genetics</subject><subject>Cytochrome b Group - metabolism</subject><subject>Electron Transport - physiology</subject><subject>Enzyme Activation</subject><subject>Enzymes</subject><subject>Genetic disorders</subject><subject>glycoproteins</subject><subject>Humans</subject><subject>Metabolites</subject><subject>Microorganisms</subject><subject>Molecular biology</subject><subject>Molecular Sequence Data</subject><subject>NAD(P)H oxidase (H2O2-forming)</subject><subject>NADPH Oxidases - chemistry</subject><subject>NADPH Oxidases - genetics</subject><subject>NADPH Oxidases - metabolism</subject><subject>Neutrophils - enzymology</subject><subject>phagocytes</subject><subject>Phosphoproteins - genetics</subject><subject>Phosphoproteins - metabolism</subject><subject>plasma membrane</subject><subject>Protein Processing, Post-Translational</subject><subject>Protein Structure, Secondary</subject><subject>Protein Subunits</subject><subject>Proteins</subject><subject>rac GTP-Binding Proteins - metabolism</subject><subject>rap1 GTP-Binding Proteins - metabolism</subject><subject>respiratory burst</subject><subject>signal transduction</subject><subject>Structure-Activity Relationship</subject><subject>superoxide anion</subject><subject>Superoxides - metabolism</subject><subject>water solubility</subject><issn>1420-682X</issn><issn>1420-9071</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNp9kc1u1DAUhS0Eoj_wAGxQxAJ1E3qvnfG12aCqtLRSVVgMUneW67FnUk2cwU6q8vY4mlEpLLrytf2do2Mfxt4hfEIAOs4AgKoG4LWacaj1C7aPzTQA4cvdLBW_2WMHOd8VeKa4fM32kDcNkKR9Np-vfJXHjU_9Q7vw9dJHn-zQxmV1ffL1x0U1HdvsP1d5SKMbxmTXlc0b74Zc2biorBva-yLoY9V5t7Kxzd0b9irYdfZvd-sh-3l-Nj-9qK--f7s8Pbmq3YxgqCl4rdDdopQioG40WSKyKKzUQXLZhKA8CrSSCAJNGxAkgwIF2i1QHLIvW9_NeNv5hfNxKPHMJrWdTb9Nb1vz701sV2bZ3xtEIahpRHH4uHNI_a_R58F0bXZ-vbbR92M2xKUmIVUBj54FBc5KNK6JCvrhP_SuH1MsH2E0F0JBIyYIt5BLfc7Jh8fUCGYq12zLNaVcM5VrdNG8f_rcv4pdm-IPIm-fiA</recordid><startdate>20021001</startdate><enddate>20021001</enddate><creator>Vignais, P V</creator><general>Springer Nature B.V</general><general>Birkhäuser Verlag</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SS</scope><scope>7T5</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U7</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PATMY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PYCSY</scope><scope>Q9U</scope><scope>RC3</scope><scope>7S9</scope><scope>L.6</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20021001</creationdate><title>The superoxide-generating NADPH oxidase: structural aspects and activation mechanism</title><author>Vignais, P V</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c570t-7fe981cb1663f19497a777a13a69f6264ff8e131a6770f7f8e10376f80809cd13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Binding Sites</topic><topic>Biosynthesis</topic><topic>Cellular biology</topic><topic>Cytochrome b Group - chemistry</topic><topic>Cytochrome b Group - genetics</topic><topic>Cytochrome b Group - metabolism</topic><topic>Electron Transport - physiology</topic><topic>Enzyme Activation</topic><topic>Enzymes</topic><topic>Genetic disorders</topic><topic>glycoproteins</topic><topic>Humans</topic><topic>Metabolites</topic><topic>Microorganisms</topic><topic>Molecular biology</topic><topic>Molecular Sequence Data</topic><topic>NAD(P)H oxidase (H2O2-forming)</topic><topic>NADPH Oxidases - chemistry</topic><topic>NADPH Oxidases - genetics</topic><topic>NADPH Oxidases - metabolism</topic><topic>Neutrophils - enzymology</topic><topic>phagocytes</topic><topic>Phosphoproteins - genetics</topic><topic>Phosphoproteins - metabolism</topic><topic>plasma membrane</topic><topic>Protein Processing, Post-Translational</topic><topic>Protein Structure, Secondary</topic><topic>Protein Subunits</topic><topic>Proteins</topic><topic>rac GTP-Binding Proteins - metabolism</topic><topic>rap1 GTP-Binding Proteins - metabolism</topic><topic>respiratory burst</topic><topic>signal transduction</topic><topic>Structure-Activity Relationship</topic><topic>superoxide anion</topic><topic>Superoxides - metabolism</topic><topic>water solubility</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Vignais, P V</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Agricultural Science Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environmental Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Environmental Science Collection</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Cellular and molecular life sciences : CMLS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Vignais, P V</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The superoxide-generating NADPH oxidase: structural aspects and activation mechanism</atitle><jtitle>Cellular and molecular life sciences : CMLS</jtitle><addtitle>Cell Mol Life Sci</addtitle><date>2002-10-01</date><risdate>2002</risdate><volume>59</volume><issue>9</issue><spage>1428</spage><epage>1459</epage><pages>1428-1459</pages><issn>1420-682X</issn><eissn>1420-9071</eissn><abstract>Flavocytochrome b558 is the catalytic core of the respiratory-burst oxidase, an enzyme complex that catalyzes the NADPH-dependent reduction of O2 into the superoxide anion O2 in phagocytic cells. Flavocytochrome b558 is anchored in the plasma membrane. It is a heterodimer that consists of a large glycoprotein gp91phox (phox forphagocyte oxidase) (beta subunit) and a small protein p22phox (alpha subunit). The other components of the respiratory-burst oxidase are water-soluble proteins of cytosolic origin, namely p67phox, p47phox, p40phox and Rac. Upon cell stimulation, they assemble with the membrane-bound flavocytochrome b558 which becomes activated and generates O2-. A defect in any of the genes encoding gp91phox, p22phox, p67phox or p47phox results in chronic granulomatous disease, a genetic disorder characterized by severe and recurrent infections, illustrating the role of O2- and the derived metabolites H2O2 and HOCl in host defense against invading microorganisms. The electron carriers, FAD and hemes b, and the binding site for NADPH are confined to the gp91phox subunit of flavocytochrome b558. The p22phox subunit serves as a docking site for the cytoso lic phox proteins. This review provides an overview of current knowledge on the structural organization of the O2(-)-generating flavocytochrome b558, its kinetics, its mechanism of activation and the regulation of its biosynthesis. Homologues of gp91phox, called Nox and Duox, are present in a large variety of non-phagocytic cells. They exhibit modest O2(-)-generating oxidase activity, and some act as proton channels. Their role in various aspects of signal transduction is currently under investigation and is briefly discussed.</abstract><cop>Switzerland</cop><pub>Springer Nature B.V</pub><pmid>12440767</pmid><doi>10.1007/s00018-002-8520-9</doi><tpages>32</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Animals Binding Sites Biosynthesis Cellular biology Cytochrome b Group - chemistry Cytochrome b Group - genetics Cytochrome b Group - metabolism Electron Transport - physiology Enzyme Activation Enzymes Genetic disorders glycoproteins Humans Metabolites Microorganisms Molecular biology Molecular Sequence Data NAD(P)H oxidase (H2O2-forming) NADPH Oxidases - chemistry NADPH Oxidases - genetics NADPH Oxidases - metabolism Neutrophils - enzymology phagocytes Phosphoproteins - genetics Phosphoproteins - metabolism plasma membrane Protein Processing, Post-Translational Protein Structure, Secondary Protein Subunits Proteins rac GTP-Binding Proteins - metabolism rap1 GTP-Binding Proteins - metabolism respiratory burst signal transduction Structure-Activity Relationship superoxide anion Superoxides - metabolism water solubility |
| title | The superoxide-generating NADPH oxidase: structural aspects and activation mechanism |
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