Cytochrome c Oxidase at Full Thrust: Regulation and Biological Consequences to Flying Insects
| Autor: | Carlos Frederico Leite Fontes, Julio A. Mignaco, Marcos A. Vannier-Santos, Marcus F. Oliveira, Luciana E S F Machado, A. Gaviraghi, Rafael D. Mesquita, Renata L.S. Goncalves |
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| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
0301 basic medicine
Enzyme complex Insecta Bioenergetics In silico Allosteric regulation oxidative phosphorylation Adenylate kinase Review Oxidative phosphorylation Biology migration bioenergetics Electron Transport Complex IV 03 medical and health sciences 0302 clinical medicine homeostasis Animals Cytochrome c oxidase dispersal lcsh:QH301-705.5 allostery phosphomimetic General Medicine Cell biology 030104 developmental biology lcsh:Biology (General) kinetics redox biology.protein Oxidation-Reduction metabolism 030217 neurology & neurosurgery Function (biology) respiration |
| Zdroj: | Cells, Vol 10, Iss 470, p 470 (2021) Cells |
| ISSN: | 2073-4409 |
| Popis: | Flight dispersal represents a key aspect of the evolutionary and ecological success of insects, allowing escape from predators, mating, and colonization of new niches. The huge energy demand posed by flight activity is essentially met by oxidative phosphorylation (OXPHOS) in flight muscle mitochondria. In insects, mitochondrial ATP supply and oxidant production are regulated by several factors, including the energy demand exerted by changes in adenylate balance. Indeed, adenylate directly regulates OXPHOS by targeting both chemiosmotic ATP production and the activities of specific mitochondrial enzymes. In several organisms, cytochrome c oxidase (COX) is regulated at transcriptional, post-translational, and allosteric levels, impacting mitochondrial energy metabolism, and redox balance. This review will present the concepts on how COX function contributes to flying insect biology, focusing on the existing examples in the literature where its structure and activity are regulated not only by physiological and environmental factors but also how changes in its activity impacts insect biology. We also performed in silico sequence analyses and determined the structure models of three COX subunits (IV, VIa, and VIc) from different insect species to compare with mammalian orthologs. We observed that the sequences and structure models of COXIV, COXVIa, and COXVIc were quite similar to their mammalian counterparts. Remarkably, specific substitutions to phosphomimetic amino acids at critical phosphorylation sites emerge as hallmarks on insect COX sequences, suggesting a new regulatory mechanism of COX activity. Therefore, by providing a physiological and bioenergetic framework of COX regulation in such metabolically extreme models, we hope to expand the knowledge of this critical enzyme complex and the potential consequences for insect dispersal. |
| Databáze: | OpenAIRE |
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