Architecture of the NADPH oxidase family of enzymes.

Blessing C Ogboo, Uriy V Grabovyy, Aniket Maini, Scott Scouten, Albert van der Vliet, Andrea Mattevi, David E Heppner

Redox biology 2022 Jun

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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. Copyright © 2022 The Authors. Published by Elsevier B.V. All rights reserved.

Citation

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. 2022 Jun;52:102298