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Part of the book series: Advances in Photosynthesis and Respiration ((AIPH,volume 39))

Summary

Quinol oxidases catalyze the four-electron reduction of oxygen to water using electrons provided by a quinol. Examples of such oxidases can be found in all kingdoms of life and within several unrelated protein families including the heme-copper oxidase family, the cytochrome bd family and the di-iron carboxylate family. In prokaryotes, there are examples of quinol oxidases from each of these families. However, only quinol oxidases of the di-iron carboxylate type are found in eukaryotes. These include the mitochondrial-localized alternative oxidase and the plastid-localized plastoquinol terminal oxidase. The quinol oxidases differ in terms of their impact on energy conservation. In general, quinol oxidases may aid in maintaining metabolic homeostasis by providing some additional flexibility in systems coupling energy and carbon metabolism.

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Abbreviations

AOX:

– Alternative oxidase;

Cyt:

– Cytochrome;

EPR:

– Electron paramagnetic resonance;

FTIR:

– Fourier transform infrared spectroscopy;

O2Red:

– Dioxygen reductases;

PTOX:

– Plastoquinol terminal oxidase;

ROS:

– Reactive oxygen species

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Acknowledgments

Both authors acknowledge financial support from the Natural Sciences and Engineering Research Council of Canada (NSERC) and A.E.M. acknowledges the support of the Faculty of Science, Wilfrid Laurier University.

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Correspondence to Allison E. McDonald .

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McDonald, A.E., Vanlerberghe, G.C. (2014). Quinol Oxidases. In: Hohmann-Marriott, M. (eds) The Structural Basis of Biological Energy Generation. Advances in Photosynthesis and Respiration, vol 39. Springer, Dordrecht. https://doi.org/10.1007/978-94-017-8742-0_9

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