The alternative oxidases (AOXs) are ubiquinol-oxidoreductases that are members of the diiron carboxylate superfamily. They are not only ubiquitously distributed within the plant kingdom but also found in increasing numbers within the fungal, protist, animal and prokaryotic kingdoms. Although functions of AOXs are highly diverse in general, they tend to play key roles in thermogenesis, stress tolerance (through the management of radical oxygen species) and the maintenance of mitochondrial and cellular energy homeostasis. The best structurally characterised AOX is from Trypanosoma brucei. In this review, we compare the structure of AOXs, created using homology modelling, from many important species in an attempt to explain differences in activity and sensitivity to AOX inhibitors. We discuss the implications of these findings not only for future structure-based drug design but also for the design of novel AOXs for gene therapy.
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Cover Image
Cover Image
An artistic model of the ‘molecular scissor’ ADAM10 (displayed in orange) at the cell surface, shown cleaving one of its substrates (green). ADAM10 is regulated by one of six TspanC8 tetraspanins (displayed in white or blue). The TspanC8s have distinct mechanisms of binding to ADAM10 and appear to dictate its substrate specificity. For more information, please see pages 719–730 in this issue of the Biochemical Society Transactions. Designer: Justyna Szyroka Artist: Eduardo Oliveira - Graphics Designer and Animator. Image kindly provided by Michael G Tomlinson.
Structural insights into the alternative oxidases: are all oxidases made equal?
Benjamin May, Luke Young, Anthony L. Moore; Structural insights into the alternative oxidases: are all oxidases made equal?. Biochem Soc Trans 15 June 2017; 45 (3): 731–740. doi: https://doi.org/10.1042/BST20160178
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