Oxidative Processes and Antioxidative Metaloenzymes

Vašková, Janka; Vaško, Ladislav; Kron, Ivan

doi:10.5772/50995

Cited by 9 publications

(7 citation statements)

References 204 publications

(211 reference statements)

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“…In addition, H2O2 can be formed by D-amino acid oxidase, urate oxidase, flavin oxidase, L-α-hydroxy acid oxidase, and fatty acyl-CoA oxidase, and by cell wall peroxidases. Reactive OH • is produced from the reaction of O2 •− and H2O2 at neutral pH and ambient temperature (Haber-Weiss reaction) or from H2O2 during the Fenton reaction [96]. In contrast, the addition of a proton (H + ) to O2 •− generates perhyroxyl radicals (HO2 • ).…”

Section: Generation and Detoxification Of Rosmentioning

confidence: 99%

Antioxidant Production in Dunaliella

2021

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Microalgae have become an attractive natural source of a diverse range of biomolecules, including enzymatic and non-enzymatic antioxidants; nevertheless, economically sustainable production of such compounds from microalgae biomass is still challenging. The main hurdles are: (a) increasing microalgae yield; (b) achieving optimal cultivation conditions; (c) energy-efficient and cost-effective downstream processing (extraction and purification); (d) optimal storage of post-processed antioxidant molecules. This review provides a detailed overview of enzymatic and non-enzymatic antioxidants in the cellular metabolism of the commercially important microalgae Dunaliella, industrial applications of antioxidant enzymes, strategies to enhanced antioxidant accumulation in cells, and the opportunities and limitations of current technologies for antioxidant enzymes production from microalgae biomass as an alternative to common microbial sources.

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Section: Generation and Detoxification Of Rosmentioning

confidence: 99%

Antioxidant Production in Dunaliella

2021

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“…The substrates are therefore hydroxylated by H 2 O at the molybdenum site as the electrons travel toward two Fe‐S residues to FAD. Reduced FAD (FADH 2 ) can thereby reoxidized by oxygen to generate hydrogen peroxide divalently, or gets reoxidized in two steps to generate two equivalents of superoxide O 2 •− univalently …”

Section: Aldehyde Oxidasementioning

confidence: 99%

Toward an Understanding of Structural Insights of Xanthine and Aldehyde Oxidases: An Overview of their Inhibitors and Role in Various Diseases

Kumar

Joshi

Kler

et al. 2017

Medicinal Research Reviews

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Almost all drug molecules become the substrates for oxidoreductase enzymes, get metabolized into more hydrophilic products and eliminated from the body. These metabolites sometime may be more potent, active, inactive, or toxic in nature compared to parent molecule. Xanthine oxidoreductase and aldehyde oxidase belong to molybdenum containing family and are well characterized for their structures and functions, in particular to their ability to oxidize/hydroxylate the xenobiotics. Their upregulated clinical levels causing oxidative stress are associated with pathways either directly involved in the progression of diseases, gout, or indirectly with the succession of other diseases such as diabetes, cancer, etc. Herein, we have put forth a comprehensive review on the xanthine and aldehyde oxidases pertaining to their structures, functions, pathophysiological role, and a comparative analysis of structural insights of xanthine and aldehyde oxidases' binding domains with endogenous ligands or inhibitors. Though both the enzymes are molybdenum containing and are likely to share some common pathways and interact with inhibitors in a similar manner but we have focused on structural prerequisites for inhibitor specificity to both the enzymes keeping in view of the existing X-ray structures. This review also provides futuristic implications in the design of inhibitors derived from inorganic complexes or small organic molecules considering the spatial features and structural insights of both the enzymes.

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“…Instead, O 2˙− production takes place on the redox-active prosthetic groups of proteins or electron-binding proteins such as CoQH 2 , which is a kinetic factor that allows or prevents the reduction of O 2 molecules and determines the production of O 2˙− in the mitochondria [3]. The mechanism of mitochondrial production and release of H 2 O 2 and O 2˙− can be seen as described in more detail in [4]. Overall, in aerobic metabolism, the mitochondrial oxidative phosphorylation system balances the reduction of O 2 to H 2 O in maximizing ATP synthesis with the simultaneous production of ROS only to the amount required for cell signaling [5].…”

Section: Introductionmentioning

confidence: 99%

Introductory Chapter: Unregulated Mitochondrial Production of Reactive Oxygen Species in Testing the Biological Activity of Compounds

Vašková¹,

Vaško²

2019

Medicinal Chemistry

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Additional information is available at the end of the chapter Reactive oxygen species production in mitochondriaMitochondria are two membrane organelles present in all cells that have a nucleus. They are the energy center of the cells. Their primary role is the production of ATP in oxidative phosphorylation, and the basis of the aerobic oxidation is the citric acid cycle interconnection representing the final metabolic pathway of oxidation of all major nutrients to the respiratory

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Oxidative Processes and Antioxidative Metaloenzymes

Cited by 9 publications

References 204 publications

Antioxidant Production in Dunaliella

Antioxidant Production in Dunaliella

Toward an Understanding of Structural Insights of Xanthine and Aldehyde Oxidases: An Overview of their Inhibitors and Role in Various Diseases

Introductory Chapter: Unregulated Mitochondrial Production of Reactive Oxygen Species in Testing the Biological Activity of Compounds

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