Architecture of the NADPH oxidase family of enzymes

Ogboo, Blessing; Grabovyy, Uriy V; Maini, Aniket; Scouten, Scott; Vliet, Albert van der; Mattevi, A.; Heppner, David E.

doi:10.1016/j.redox.2022.102298

Cited by 42 publications

(29 citation statements)

References 27 publications

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“…(B) AlphaFold structural model of the catalytic core of the ancestral of RBOHs and calcium-independent NOXs, inferred through ancestral sequence reconstruction (see section 3 , Results and Discussion). For a general description of the NOX architecture see [ 71 ]. …”

Section: Resultsmentioning

confidence: 99%

Evolutionary and structural analyses of the NADPH oxidase family in eukaryotes reveal an initial calcium dependency

et al. 2022

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Section: Resultsmentioning

confidence: 99%

Evolutionary and structural analyses of the NADPH oxidase family in eukaryotes reveal an initial calcium dependency

et al. 2022

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“…1 A ) ( 7 , 8 , 9 ). These soluble NOXes are not related to the mammalian transmembrane reactive oxygen species (ROS)–producing NADPH oxidases (NOX1–5 and DUOX1–2) ( 10 ). The active site of a typical tDBDF superfamily NOX enzyme (∼50 kDa per monomer) consists of a single FAD cofactor and an adjacent redox-active cysteine that cycles between sulfenic acid and reduced cysteine to accomplish the four electron reductions of oxygen to water ( 7 , 11 , 12 ).…”

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confidence: 99%

A natural fusion of flavodiiron, rubredoxin, and rubredoxin oxidoreductase domains is a self-sufficient water-forming oxidase of Trichomonas vaginalis

Abdulaziz

Bell

Rashid

et al. 2022

Journal of Biological Chemistry

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“…NOX4, characterized by ubiquitous expression and continuous H 2 O 2 production ( Figure 1 and Figure 2 ), is the only isoform proposed to be constitutively active and negatively regulated by ATP [ 152 ]. The binding implies a generalized role for NOX4 in the maintenance of basal physiological redox homeostasis [ 153 ].…”

Section: Noxs and Cancermentioning

confidence: 99%

NOX as a Therapeutic Target in Liver Disease

2022

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The nicotinamide adenine dinucleotide phosphate hydrogen oxidase (NADPH oxidase or NOX) plays a critical role in the inflammatory response and fibrosis in several organs such as the lungs, pancreas, kidney, liver, and heart. In the liver, NOXs contribute, through the generation of reactive oxygen species (ROS), to hepatic fibrosis by acting through multiple pathways, including hepatic stellate cell activation, proliferation, survival, and migration of hepatic stellate cells; hepatocyte apoptosis, enhancement of fibrogenic mediators, and mediation of an inflammatory cascade in both Kupffer cells and hepatic stellate cells. ROS are overwhelmingly produced during malignant transformation and hepatic carcinogenesis (HCC), creating an oxidative microenvironment that can cause different and various types of cellular stress, including DNA damage, ER stress, cell death of damaged hepatocytes, and oxidative stress. NOX1, NOX2, and NOX4, members of the NADPH oxidase family, have been linked to the production of ROS in the liver. This review will analyze some diseases related to an increase in oxidative stress and its relationship with the NOX family, as well as discuss some therapies proposed to slow down or control the disease’s progression.

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Architecture of the NADPH oxidase family of enzymes

Cited by 42 publications

References 27 publications

Evolutionary and structural analyses of the NADPH oxidase family in eukaryotes reveal an initial calcium dependency

Evolutionary and structural analyses of the NADPH oxidase family in eukaryotes reveal an initial calcium dependency

A natural fusion of flavodiiron, rubredoxin, and rubredoxin oxidoreductase domains is a self-sufficient water-forming oxidase of Trichomonas vaginalis

NOX as a Therapeutic Target in Liver Disease

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