The DOI matches its Crossref record; 233 of the 236 references it cites were found in a registry or an index.
Alternative oxidase: Distribution, induction, properties, structure, regulation, and functions
Abstract
The respiratory chain in the majority of organisms with aerobic type metabolism features the concomitant existence of the phosphorylating cytochrome pathway and the cyanide- and antimycin A-insensitive oxidative route comprising a so-called alternative oxidase (AOX) as a terminal oxidase. In this review, the history of AOX discovery is described. Considerable evidence is presented that AOX occurs widely in organisms at various levels of organization and is not confined to the plant kingdom. This enzyme has not been found only in Archaea, mammals, some yeasts and protists. Bioinformatics research revealed the sequences characteristic of AOX in representatives of various taxonomic groups. Based on multiple alignments of these sequences, a phylogenetic tree was constructed to infer their possible evolution. The ways of AOX activation, as well as regulatory interactions between AOX and the main respiratory chain are described. Data are summarized concerning the properties of AOX and the AOX-encoding genes whose expression is either constitutive or induced by various factors. Information is presented on the structure of AOX, its active center, and the ubiquinone-binding site. The principal functions of AOX are analyzed, including the cases of cell survival, optimization of respiratory metabolism, protection against excess of reactive oxygen species, and adaptation to variable nutrition sources and to biotic and abiotic stress factors. It is emphasized that different AOX functions complement each other in many instances and are not mutually exclusive. Examples are given to demonstrate that AOX is an important tool to overcome the adverse aftereffects of restricted activity of the main respiratory chain in cells and whole animals. This is the first comprehensive review on alternative oxidases of various organisms ranging from yeasts and protists to vascular plants.
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“CaAoxp is thought to be an enzyme protecting against ROS (Yan et al. 2009; Rogov et al. 2014), which might be relevant, as dysfunctional Cl and CIII generate more free oxygen radicals (Li et al. 2011).”
From Candida albicans PPR proteins are required for the expression of respiratory Complex I subunits (2024) · cites this paper as Rogov et al. 2014
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Metadata
- Authors
- Rogov, A. G., Sukhanova, E. I., Uralskaya, L. A., Aliverdieva, D. A., & Zvyagilskaya, R. A.
- Affiliations
- Russian Academy of Sciences (RU)
- Corresponding author
- Rogov, A. G.
- Venue
- Biochemistry (Moscow)
- Publisher
- Pleiades Publishing Ltd
- Published
- 2014-12
- Volume
- 79
- Issue
- 13
- Pages
- 1615-1634
- ISSN
- 0006-2979 (ISSN-L)
- 1608-3040
- OpenAlex
- W2135673284
- Cited by
- 73
- References
- 236
- Citations by year
- 2026: 2 · 2025: 7 · 2024: 8 · 2023: 2 · 2022: 8 · 2021: 7 · 2020: 8 · 2019: 8 · 2018: 11 · 2017: 7 · 2016: 2 · 2015: 2
- FWCI
- 0.35
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Biochemistry (Moscow) (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- alternative oxidase, electron transport chain, terminal oxidase, active site, ubiquinone binding site, stress adaptation, cytochrome pathway, cyanide-resistant respiration
- MeSH terms
- Alternative Oxidase, Bacteria, Electron Transport, Nutritional Physiological Phenomena, Oxidoreductases, Phylogeny, Plant Proteins, Protein Conformation, Mitochondrial Proteins
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