Authors
Laurence Prunetti, Pascale Infossi, Myriam Brugna, Christine Ebel, Marie-Thérèse Giudici-Orticoni, Marianne Guiral
Publication date
2010/12/31
Journal
Journal of Biological Chemistry
Volume
285
Issue
53
Pages
41815-41826
Publisher
American Society for Biochemistry and Molecular Biology
Description
Aquifex aeolicus, a hyperthermophilic and microaerophilic bacterium, obtains energy for growth from inorganic compounds alone. It was previously proposed that one of the respiratory pathways in this organism consists of the electron transfer from hydrogen sulfide (H2S) to molecular oxygen. H2S is oxidized by the sulfide quinone reductase, a membrane-bound flavoenzyme, which reduces the quinone pool. We have purified and characterized a novel membrane-bound multienzyme supercomplex that brings together all the molecular components involved in this bioenergetic chain. Our results indicate that this purified structure consists of one dimeric bc1 complex (complex III), one cytochrome c oxidase (complex IV), and one or two sulfide quinone reductases as well as traces of the monoheme cytochrome c555 and quinone molecules. In addition, this work strongly suggests that the cytochrome c oxidase in the …
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