scholarly journals Alternative oxidase: an inter-kingdom perspective on the function and regulation of this broadly distributed 'cyanide-resistant' terminal oxidase

2008 ◽  
Vol 35 (7) ◽  
pp. 535 ◽  
Author(s):  
Allison E. McDonald
Keyword(s):  
Translational Regulation ◽  
Alternative Oxidase ◽  
Physiological Function ◽  
Comparative Approach ◽  
Terminal Oxidase ◽  
Transcriptional Expression ◽  
Inner Mitochondrial Membrane ◽  
Respiratory Pathway ◽  
Quinol Oxidase ◽  
Transport Chain

Alternative oxidase (AOX) is a terminal quinol oxidase located in the respiratory electron transport chain that catalyses the oxidation of quinol and the reduction of oxygen to water. However, unlike the cytochrome c oxidase respiratory pathway, the AOX pathway moves fewer protons across the inner mitochondrial membrane to generate a proton motive force that can be used to synthesise ATP. The energy passed to AOX is dissipated as heat. This appears to be very wasteful from an energetic perspective and it is likely that AOX fulfils some physiological function(s) that makes up for its apparent energetic shortcomings. An examination of the known taxonomic distribution of AOX and the specific organisms in which AOX has been studied has been used to explore themes pertaining to AOX function and regulation. A comparative approach was used to examine AOX function as it relates to the biochemical function of the enzyme as a quinol oxidase and associated topics, such as enzyme structure, catalysis and transcriptional expression and post-translational regulation. Hypotheses that have been put forward about the physiological function(s) of AOX were explored in light of some recent discoveries made with regard to species that contain AOX. Fruitful areas of research for the AOX community in the future have been highlighted.

scholarly journals Legume Alternative Oxidase Isoforms Show Differential Sensitivity to Pyruvate Activation

2022 ◽  
Vol 12 ◽  
Author(s):  
Crystal Sweetman ◽  
Jennifer Selinski ◽  
Troy K. Miller ◽  
James Whelan ◽  
David A. Day
Keyword(s):  
Stress Responses ◽  
Alternative Oxidase ◽  
Differential Sensitivity ◽  
Respiratory Pathway ◽  
Activation Kinetics ◽  
Transport Chain ◽  
Wide Range ◽  
Selective Expression ◽  
Energy Conserving ◽  
Very High

Alternative oxidase (AOX) is an important component of the plant respiratory pathway, enabling a route for electrons that bypasses the energy-conserving, ROS-producing complexes of the mitochondrial electron transport chain. Plants contain numerous isoforms of AOX, classified as either AOX1 or AOX2. AOX1 isoforms have received the most attention due to their importance in stress responses across a wide range of species. However, the propensity for at least one isoform of AOX2 to accumulate to very high levels in photosynthetic tissues of all legumes studied to date, suggests that this isoform has specialized roles, but we know little of its properties. Previous studies with sub-mitochondrial particles of soybean cotyledons and roots indicated that differential expression of GmAOX1, GmAOX2A, and GmAOX2D across tissues might confer different activation kinetics with pyruvate. We have investigated this using recombinantly expressed isoforms of soybean AOX in a previously described bacterial system (Selinski et al., 2016, Physiologia Plantarum 157, 264-279). Pyruvate activation kinetics were similar between the two GmAOX2 isoforms but differed substantially from those of GmAOX1, suggesting that selective expression of AOX1 and 2 could determine the level of AOX activity. However, this alone cannot completely explain the differences seen in sub-mitochondrial particles isolated from different legume tissues and possible reasons for this are discussed.

scholarly journals The oxidation of nicotinic acid by Pseudomonas ovalis Chester. The terminal oxidase

1972 ◽  
Vol 129 (3) ◽  
pp. 755-761 ◽  
Author(s):  
M. V. Jones ◽  
D. E. Hughes
Keyword(s):  
Electron Transport ◽  
Nicotinic Acid ◽  
Electron Transport Chain ◽  
Acid Oxidase ◽  
Terminal Oxidase ◽  
Difference Spectra ◽  
Terminal Oxidases ◽  
Cytochrome O ◽  
Transport Chain ◽  
Terminal Oxidation

In cell-free extracts of Pseudomonas ovalis nicotinic acid oxidase is confined to the wallmembrane fraction. It is associated with an electron-transport chain comprising b- and c-type cytochromes only, differing proportions of which are reduced by nicotinate and NADH. CO difference-spectra show two CO-binding pigments, cytochrome o (absorption maximum at 417nm) and another component absorbing maximally at 425nm. Cytochrome o is not reduced by NADH or by succinate but is by nicotinate, which can also reduce the ‘425’ CO-binding pigment. The effects of inhibitors of terminal oxidation support the idea of two terminal oxidases and a scheme involving the ‘425’ CO-binding pigment and the other components of the electron-transport chain is proposed.

A Functional Alternative Oxidase Modulates Plant Salt Tolerance in Physcomitrella patens

2019 ◽  
Vol 60 (8) ◽  
pp. 1829-1841 ◽  
Author(s):  
Guochun Wu ◽  
Sha Li ◽  
Xiaochuan Li ◽  
Yunhong Liu ◽  
Shuangshuang Zhao ◽  
...  
Keyword(s):  
Salt Stress ◽  
Salt Tolerance ◽  
Stress Responses ◽  
Alternative Oxidase ◽  
Physcomitrella Patens ◽  
Redox Homeostasis ◽  
Respiratory Pathway ◽  
Functional Link ◽  
Salt Stress Condition ◽  
Plant Salt Tolerance

Abstract Alternative oxidase (AOX) has been reported to be involved in mitochondrial function and redox homeostasis, thus playing an essential role in plant growth as well as stress responses. However, its biological functions in nonseed plants have not been well characterized. Here, we report that AOX participates in plant salt tolerance regulation in moss Physcomitrella patens (P. patens). AOX is highly conserved and localizes to mitochondria in P. patens. We observed that PpAOX rescued the impaired cyanide (CN)-resistant alternative (Alt) respiratory pathway in Arabidopsis thaliana (Arabidopsis) aox1a mutant. PpAOX transcription and Alt respiration were induced upon salt stress in P. patens. Using homologous recombination, we generated PpAOX-overexpressing lines (PpAOX OX). PpAOX OX plants exhibited higher Alt respiration and lower total reactive oxygen species accumulation under salt stress condition. Strikingly, we observed that PpAOX OX plants displayed decreased salt tolerance. Overexpression of PpAOX disturbed redox homeostasis in chloroplasts. Meanwhile, chloroplast structure was adversely affected in PpAOX OX plants in contrast to wild-type (WT) P. patens. We found that photosynthetic activity in PpAOX OX plants was also lower compared with that in WT. Together, our work revealed that AOX participates in plant salt tolerance in P. patens and there is a functional link between mitochondria and chloroplast under challenging conditions.

scholarly journals Alternative Oxidase Inhibition Impairs Tobacco Root Development and Root Hair Formation

2021 ◽  
Vol 12 ◽  
Author(s):  
Yang Liu ◽  
Lu-Lu Yu ◽  
Ye Peng ◽  
Xin-Xin Geng ◽  
Fei Xu
Keyword(s):  
Gene Expression ◽  
Root Development ◽  
Transcriptome Analysis ◽  
Root Hair ◽  
Alternative Oxidase ◽  
Regulation Of Gene Expression ◽  
Main Root ◽  
Respiratory Pathway ◽  
Root Hair Formation ◽  
Hair Formation

Alternative oxidase (AOX) is the terminal oxidase of the mitochondrial respiratory electron transport chain in plant cells and is critical for the balance of mitochondrial hemostasis. In this study, the effect of inhibition of AOX with different concentrations of salicylhydroxamic acid (SHAM) on the tobacco root development was investigated. We show here that AOX inhibition significantly impaired the development of the main root and root hair formation of tobacco. The length of the main root of SHAM-treated tobacco was significantly shorter than that of the control, and no root hairs were formed after treatment with a concentration of 1 mM SHAM or more. The transcriptome analysis showed that AOX inhibition by 1 mM SHAM involved in the regulation of gene expression related to root architecture. A total of 5,855 differentially expressed genes (DEGs) were obtained by comparing SHAM-treated roots with control. Of these, the gene expression related to auxin biosynthesis and perception were significantly downregulated by 1 mM SHAM. Similarly, genes related to cell wall loosening, cell cycle, and root meristem growth factor 1 (RGF1) also showed downregulation on SHAM treatment. Moreover, combined with the results of physiological measurements, the transcriptome analysis demonstrated that AOX inhibition resulted in excessive accumulation of reactive oxygen species in roots, which further induced oxidative damage and cell apoptosis. It is worth noting that when indoleacetic acid (20 nM) and dimethylthiourea (10 mM) were added to the medium containing SHAM, the defects of tobacco root development were alleviated, but to a limited extent. Together, these findings indicated that AOX-mediated respiratory pathway plays a crucial role in the tobacco root development, including root hair formation.

Cloning and Analysis of the Alternative Oxidase Gene of Neurospora crassa

Genetics ◽  
1996 ◽  
Vol 142 (1) ◽  
pp. 129-140 ◽  
Author(s):  
Qiuhong Li ◽  
R Gary Ritzel ◽  
Lesley L T McLean ◽  
Lee McIntosh ◽  
Tak Ko ◽  
...  
Keyword(s):  
Neurospora Crassa ◽  
Alternative Oxidase ◽  
Electron Flow ◽  
Mitochondrial Protein ◽  
Transcriptional Level ◽  
Wild Type ◽  
Respiratory Pathway ◽  
Oxidase Gene ◽  
Alternative Respiratory Pathway ◽  
Cytochrome Pathway

Mitochondria of Neurospora crassa contain a cyanide-resistant alternative respiratory pathway in addition to the cytochrome pathway. The alternative oxidase is present only when electron flow through the cytochrome chain is restricted. Both genomic and cDNA copies for the alternative oxidase gene have been isolated and analyzed. The sequence of the predicted protein is homologous to that of other species. The mRNA for the alternative oxidase is scarce in wild-type cultures grown under normal conditions, but it is abundant in cultures grown in the presence of chloramphenicol, an inhibitor of mitochondrial protein synthesis, or in mutants deficient in mitochondrial cytochromes. Thus, induction of alternative oxidase appears to be at the transcriptional level. Restriction fragment length polymorphism mapping of the isolated gene demonstrated that it is located in a position corresponding to the aod-1 locus. Sequence analysis of mutant aod-1 alleles reveals mutations affecting the coding sequence of the alternative oxidase. The level of aod-1 mRNA in an aod-2 mutant strain that had been grown in the presence of chloramphenicol was reduced several fold relative to wild-type, supporting the hypothesis that the product of aod-2 is required for optimal expression of aod-1.

scholarly journals Research journey of respirasome

2020 ◽  
Vol 11 (5) ◽  
pp. 318-338 ◽  
Author(s):  
Meng Wu ◽  
Jinke Gu ◽  
Shuai Zong ◽  
Runyu Guo ◽  
Tianya Liu ◽  
...  
Keyword(s):  
Short Review ◽  
Research Field ◽  
Atomic Scale ◽  
Inner Mitochondrial Membrane ◽  
Macroscopic Scale ◽  
The Past ◽  
Transport Chain ◽  
High Resolution Structure ◽  
New Perspective ◽  
Resolution Structure

AbstractRespirasome, as a vital part of the oxidative phosphorylation system, undertakes the task of transferring electrons from the electron donors to oxygen and produces a proton concentration gradient across the inner mitochondrial membrane through the coupled translocation of protons. Copious research has been carried out on this lynchpin of respiration. From the discovery of individual respiratory complexes to the report of the high-resolution structure of mammalian respiratory supercomplex I1III2IV1, scientists have gradually uncovered the mysterious veil of the electron transport chain (ETC). With the discovery of the mammalian respiratory mega complex I2III2IV2, a new perspective emerges in the research field of the ETC. Behind these advances glitters the light of the revolution in both theory and technology. Here, we give a short review about how scientists ‘see’ the structure and the mechanism of respirasome from the macroscopic scale to the atomic scale during the past decades.

Arabidopsis mtHSC70-1 plays important roles in the establishment of COX-dependent respiration and redox homeostasis

2019 ◽  
Vol 70 (20) ◽  
pp. 5575-5590 ◽  
Author(s):  
Shan-Shan Wei ◽  
Wei-Tao Niu ◽  
Xiao-Ting Zhai ◽  
Wei-Qian Liang ◽  
Meng Xu ◽  
...  
Keyword(s):  
Alternative Oxidase ◽  
Redox Homeostasis ◽  
Superoxide Dismutase 1 ◽  
Respiratory Pathway ◽  
Cellular Processes ◽  
Growth Defects ◽  
Alternative Respiratory Pathway ◽  
Abnormal Mitochondria ◽  
Shock Proteins ◽  
Severe Growth

Abstract The 70 kDa heat shock proteins function as molecular chaperones and are involved in diverse cellular processes. However, the functions of the plant mitochondrial HSP70s (mtHSC70s) remain unclear. Severe growth defects were observed in the Arabidopsis thaliana mtHSC70-1 knockout lines, mthsc70-1a and mthsc70-1b. Conversely, the introduction of the mtHSC70-1 gene into the mthsc70-1a background fully reversed the phenotypes, indicating that mtHSC70-1 is essential for plant growth. The loss of mtHSC70-1 functions resulted in abnormal mitochondria and alterations to respiration because of an inhibition of the cytochrome c oxidase (COX) pathway and the activation of the alternative respiratory pathway. Defects in COX assembly were observed in the mtHSC70-1 knockout lines, leading to decreased COX activity. The mtHSC70-1 knockout plants have increased levels of reactive oxygen species (ROS). The introduction of the Mn-superoxide dismutase 1 (MSD1) or the catalase 1 (CAT1) gene into the mthsc70-1a plants decreased ROS levels, reduced the expression of alternative oxidase, and partially rescued growth. Taken together, our data suggest that mtHSC70-1 plays important roles in the establishment of COX-dependent respiration.

The Electron Transport Chain

2014 ◽  
Vol 76 (7) ◽  
pp. 456-458 ◽  
Author(s):  
Chris Romero ◽  
James Choun
Keyword(s):  
Electron Transport ◽  
Advanced Placement ◽  
Electron Transport Chain ◽  
Cellular Respiration ◽  
College Level ◽  
Inner Mitochondrial Membrane ◽  
College Biology ◽  
Everyday Objects ◽  
Transport Chain ◽  
Introductory College

This activity provides students an interactive demonstration of the electron transport chain and chemiosmosis during aerobic respiration. Students use simple, everyday objects as hydrogen ions and electrons and play the roles of the various proteins embedded in the inner mitochondrial membrane to show how this specific process in cellular respiration produces ATP. The activity works best as a supplement after you have already discussed the electron transport chain in lecture but can be used prior to instruction to help students visualize the processes that occur. This demonstration was designed for general college biology for majors at a community college, but it could be used in any introductory college-level or advanced placement biology course.

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