scholarly journals Beyond Ethylene: New Insights Regarding the Role of Alternative Oxidase in the Respiratory Climacteric

2020 ◽  
Vol 11 ◽  
Author(s):  
Seanna Hewitt ◽  
Amit Dhingra
Keyword(s):  
2018 ◽  
Vol 56 (4) ◽  
pp. 1297-1303 ◽  
Author(s):  
W. H. Hu ◽  
X. H. Yan ◽  
Y. He ◽  
X. L. Ye

2005 ◽  
Vol 56 (416) ◽  
pp. 1499-1515 ◽  
Author(s):  
Stephen M. Sieger ◽  
Brian K. Kristensen ◽  
Christine A. Robson ◽  
Sasan Amirsadeghi ◽  
Edward W. Y. Eng ◽  
...  

2001 ◽  
Vol 21 (3) ◽  
pp. 369-379 ◽  
Author(s):  
Vasily N. Popov ◽  
Albert C. Purvis ◽  
Vladimir P. Skulachev ◽  
Anneke M. Wagner

We have investigated the influence of stress conditions such as incubation at 4°C and incubation in hyperoxygen atmosphere, on plant tissues. The ubiquinone (Q) content and respiratory activity of purified mitochondria was studied. The rate of respiration of mitochondria isolated from cold-treated green bell peppers (Capsicum annuum L) exceeds that of controls, but this is not so for mitochondria isolated from cold-treated cauliflower (Brassica oleracea L). Treatment with high oxygen does not alter respiration rates of cauliflower mitochondria. Analysis of kinetic data relating oxygen uptake with Q reduction in mitochondria isolated from tissue incubated at 4°C (bell peppers and cauliflowers) and at high oxygen levels (cauliflowers) reveals an increase in the total amount of Q and in the percentage of inoxidizable QH2. The effects are not invariably accompanied by an induction of the alternative oxidase (AOX). In those mitochondria where the AOX is induced (cold-treated bell pepper and cauliflower treated with high oxygen) superoxide production is lower than in the control. The role of reduced Q accumulation and AOX induction in the defense against oxidative damage is discussed.


1997 ◽  
Vol 17 (3) ◽  
pp. 319-333 ◽  
Author(s):  
Anneke M. Wagner ◽  
Anthony L. Moore

Current understanding of the structure and function of the plant alternative oxidase is reviewed. In particular, the role of the oxidase in the protection of tissues against oxidative stress is developed.


2016 ◽  
Vol 212 (1) ◽  
pp. 66-79 ◽  
Author(s):  
Igor Florez-Sarasa ◽  
Miquel Ribas-Carbo ◽  
Néstor Fernández Del-Saz ◽  
Kevin Schwahn ◽  
Zoran Nikoloski ◽  
...  

Parasitology ◽  
2010 ◽  
Vol 137 (6) ◽  
pp. 899-917 ◽  
Author(s):  
M. C. TAYLOR ◽  
J. M. KELLY

SUMMARYIron is almost ubiquitous in living organisms due to the utility of its redox chemistry. It is also dangerous as it can catalyse the formation of reactive free radicals – a classical double-edged sword. In this review, we examine the uptake and usage of iron by trypanosomatids and discuss how modulation of host iron metabolism plays an important role in the protective response. Trypanosomatids require iron for crucial processes including DNA replication, antioxidant defence, mitochondrial respiration, synthesis of the modified base J and, in African trypanosomes, the alternative oxidase. The source of iron varies between species. Bloodstream-form African trypanosomes acquire iron from their host by uptake of transferrin, andLeishmania amazonensisexpresses a ZIP family cation transporter in the plasma membrane. In other trypanosomatids, iron uptake has been poorly characterized. Iron-withholding responses by the host can be a major determinant of disease outcome. Their role in trypanosomatid infections is becoming apparent. For example, the cytosolic sequestration properties of NRAMP1, confer resistance against leishmaniasis. Conversely, cytoplasmic sequestration of iron may be favourable rather than detrimental toTrypanosoma cruzi. The central role of iron in both parasite metabolism and the host response is attracting interest as a possible point of therapeutic intervention.


Microbiology ◽  
2014 ◽  
Vol 160 (9) ◽  
pp. 2045-2052 ◽  
Author(s):  
Elina Balodite ◽  
Inese Strazdina ◽  
Nina Galinina ◽  
Samantha McLean ◽  
Reinis Rutkis ◽  
...  

The genome of the ethanol-producing bacterium Zymomonas mobilis encodes a bd-type terminal oxidase, cytochrome bc 1 complex and several c-type cytochromes, yet lacks sequences homologous to any of the known bacterial cytochrome c oxidase genes. Recently, it was suggested that a putative respiratory cytochrome c peroxidase, receiving electrons from the cytochrome bc 1 complex via cytochrome c 552, might function as a peroxidase and/or an alternative oxidase. The present study was designed to test this hypothesis, by construction of a cytochrome c peroxidase mutant (Zm6-perC), and comparison of its properties with those of a mutant defective in the cytochrome b subunit of the bc 1 complex (Zm6-cytB). Disruption of the cytochrome c peroxidase gene (ZZ60192) caused a decrease of the membrane NADH peroxidase activity, impaired the resistance of growing culture to exogenous hydrogen peroxide and hampered aerobic growth. However, this mutation did not affect the activity or oxygen affinity of the respiratory chain, or the kinetics of cytochrome d reduction. Furthermore, the peroxide resistance and membrane NADH peroxidase activity of strain Zm6-cytB had not decreased, but both the oxygen affinity of electron transport and the kinetics of cytochrome d reduction were affected. It is therefore concluded that the cytochrome c peroxidase does not terminate the cytochrome bc 1 branch of Z. mobilis, and that it is functioning as a quinol peroxidase.


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