McDonald 2011 Abstract IOC65

From Bioblast
McDonald AE (2011) Alternative oxidase respiratory capacity in eukaryotes and prokaryotes. MiPNet16.03.


McDonald AE (2011)

Event: IOC65

Alternative oxidase (AOX) is a ubiquinol terminal oxidase present in the respiratory electron transport chains of a wide variety of organisms [1]. AOX by-passes 2 of the 3 proton pumping complexes in the respiratory chain and therefore makes respiration less efficient in terms of the amount of ATP generated per oxygen consumed. Our previous work using bioinformatics has revealed the presence of AOX genes in eukaryotic organisms such as plants, animals, fungi, algae, and protists, as well as in prokaryotes in several species of eubacteria [2]. Recent work using reverse transcriptase polymerase chain reaction (RT-PCR) experiments has demonstrated that these genes are transcribed in many organisms [3]. Our focus is now shifting to exploring the respiratory capacity of AOX proteins in these different systems and in identifying how the activity of AOX proteins is regulated at the post-translational level.

β€’ Keywords: Alternative oxidase, Cyanide-resistant Respiration, Evolutionary history, post-translational regulation of protein activity


Preparation: Oxidase;biochemical oxidation 

Authors: McDonald AE (1)

Affiliations: (1) Department of Biology, Wilfrid Laurier University, Waterloo, Ontario, Canada.

References: 1. McDonald AE. (2008) Alternative oxidase: an inter-kingdom perspective on the function and regulation of this broadly distributed β€˜cyanide-resistant’ terminal oxidase. Functional Plant Biology. 35:535-552. 2. McDonald AE, and Vanlerberghe GC. 2006. Origins, Evolutionary History, and Taxonomic Distribution of Alternative Oxidase and Plastoquinol Terminal Oxidase. Comparative Biochemistry and Physiology- Part D: Genomics and Proteomics. 1: 357-364. 3. McDonald AE, Vanlerberghe, GC, and Staples JF. 2009. Alternative Oxidase in Animals: Unique Characteristics and Taxonomic Distribution. The Journal of Experimental Biology. 212: 2627-2534.

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