Architecture of the NADPH oxidase family of enzymes
The NADPH Oxidases (NOX) catalyze the deliberate production of reactive oxygen species (ROS) and are established regulators of redox-dependent processes across diverse biological settings. Proper management of their activity is controlled through a conserved electron transfer (ET) cascade from cytos...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Elsevier
2022-06-01
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| Series: | Redox Biology |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2213231722000702 |
| _version_ | 1828787328310575104 |
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| author | Blessing C. Ogboo Uriy V. Grabovyy Aniket Maini Scott Scouten Albert van der Vliet Andrea Mattevi David E. Heppner |
| author_facet | Blessing C. Ogboo Uriy V. Grabovyy Aniket Maini Scott Scouten Albert van der Vliet Andrea Mattevi David E. Heppner |
| author_sort | Blessing C. Ogboo |
| collection | DOAJ |
| description | The NADPH Oxidases (NOX) catalyze the deliberate production of reactive oxygen species (ROS) and are established regulators of redox-dependent processes across diverse biological settings. Proper management of their activity is controlled through a conserved electron transfer (ET) cascade from cytosolic NADPH substrate through the plasma membrane to extracellular O2. After decades-long investigations of their biological functions, including potential as drug targets, only very recently has atomic-resolution information of NOX enzymes been made available. In this graphical review, we summarize the present structural biology understanding of the NOX enzymes afforded by X-ray crystallography and cryo-electron microscopy. Combined molecular-level insights predominantly informed by DUOX1 full-length Cryo-EM structures suggest a general structural basis for the control of their catalytic activity by intracellular domain-domain stabilization. |
| first_indexed | 2024-12-12T00:29:27Z |
| format | Article |
| id | doaj.art-3ba2e227ebf44e6cae12dd33bd4a39a3 |
| institution | Directory Open Access Journal |
| issn | 2213-2317 |
| language | English |
| last_indexed | 2024-12-12T00:29:27Z |
| publishDate | 2022-06-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Redox Biology |
| spelling | doaj.art-3ba2e227ebf44e6cae12dd33bd4a39a32022-12-22T00:44:32ZengElsevierRedox Biology2213-23172022-06-0152102298Architecture of the NADPH oxidase family of enzymesBlessing C. Ogboo0Uriy V. Grabovyy1Aniket Maini2Scott Scouten3Albert van der Vliet4Andrea Mattevi5David E. Heppner6Department of Chemistry, University at Buffalo, The State University of New York, Buffalo, NY, USADepartment of Chemistry, University at Buffalo, The State University of New York, Buffalo, NY, USADepartment of Chemistry, University at Buffalo, The State University of New York, Buffalo, NY, USADepartment of Chemistry, University at Buffalo, The State University of New York, Buffalo, NY, USADepartment of Pathology and Laboratory Medicine, Robert Larner, M.D. College of Medicine, University of Vermont, Burlington, VT, USADepartment of Genetics and Microbiology, University of Pavia, ItalyDepartment of Chemistry, University at Buffalo, The State University of New York, Buffalo, NY, USA; Department of Pharmacology and Therapeutics, Roswell Park Comprehensive Cancer Center, Buffalo, NY, USA; Corresponding author. Natural Sciences Complex. University at Buffalo, The State University of New York. Buffalo, NY, 14260, USA.The NADPH Oxidases (NOX) catalyze the deliberate production of reactive oxygen species (ROS) and are established regulators of redox-dependent processes across diverse biological settings. Proper management of their activity is controlled through a conserved electron transfer (ET) cascade from cytosolic NADPH substrate through the plasma membrane to extracellular O2. After decades-long investigations of their biological functions, including potential as drug targets, only very recently has atomic-resolution information of NOX enzymes been made available. In this graphical review, we summarize the present structural biology understanding of the NOX enzymes afforded by X-ray crystallography and cryo-electron microscopy. Combined molecular-level insights predominantly informed by DUOX1 full-length Cryo-EM structures suggest a general structural basis for the control of their catalytic activity by intracellular domain-domain stabilization.http://www.sciencedirect.com/science/article/pii/S2213231722000702 |
| spellingShingle | Blessing C. Ogboo Uriy V. Grabovyy Aniket Maini Scott Scouten Albert van der Vliet Andrea Mattevi David E. Heppner Architecture of the NADPH oxidase family of enzymes Redox Biology |
| title | Architecture of the NADPH oxidase family of enzymes |
| title_full | Architecture of the NADPH oxidase family of enzymes |
| title_fullStr | Architecture of the NADPH oxidase family of enzymes |
| title_full_unstemmed | Architecture of the NADPH oxidase family of enzymes |
| title_short | Architecture of the NADPH oxidase family of enzymes |
| title_sort | architecture of the nadph oxidase family of enzymes |
| url | http://www.sciencedirect.com/science/article/pii/S2213231722000702 |
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