Cited by 73Mitochondrial Function and PathologyRedox biology and oxidative stressEnzyme Structure and Function

Alternative oxidase: distribution, induction, properties, structure, regulation, and functions

Rogov, A. G., Sukhanova, E. I., Uralskaya, L. A., Aliverdieva, D. A., Zvyagilskaya, R. A.·2014·Biochemistry (Moscow)

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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Crossref · 10.1134/s0006297914130112

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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)
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 · 2013: 1
FWCI
0.35
Type
journal article
Language
en
Open access
closed
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
  • Physical Sciences › Materials Science › Materials Chemistry › 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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