ArticleThe Journal of biological chemistry2010
New functional sulfide oxidase-oxygen reductase supercomplex in the membrane of the hyperthermophilic bacterium Aquifex aeolicus.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 37 citations in OpenAlex.
- Persulfide Biosynthesis Conserved Evolutionarily in All Organisms.Antioxidants & redox signaling · 2023Review
- Simultaneous sulfide and methane oxidation by an extremophile.Nature communications · 2023Article
- The Unusual Homodimer of a Heme-Copper Terminal Oxidase Allows Itself to Utilize Two Electron Donors.Angewandte Chemie (International ed. in English) · 2021Article
- Article
- A 3.3 Å-Resolution Structure of Hyperthermophilic Respiratory Complex III Reveals the Mechanism of Its Thermal Stability.Angewandte Chemie (International ed. in English) · 2020Article
- The effect of pH on the dynamics of natural membranes.The European physical journal. E, Soft matter · 2018Article
- Protein complex formation during denitrification by Pseudomonas aeruginosa.Microbial biotechnology · 2017Review
- Electrophoretic mobility of a monotopic membrane protein inserted into the top of supported lipid bilayers.The European physical journal. E, Soft matter · 2016Article
- Protein Network of the Pseudomonas aeruginosa Denitrification Apparatus.Journal of bacteriology · 2016Article
- Insertion and self-diffusion of a monotopic protein, the Aquifex aeolicus sulfide quinone reductase, in supported lipid bilayers.The European physical journal. E, Soft matter · 2015Article
- Metabolic evolution of a deep-branching hyperthermophilic chemoautotrophic bacterium.PloS one · 2014Article
- Article
- Dynamics measured by neutron scattering correlates with the organization of bioenergetics complexes in natural membranes from hyperthermophile and mesophile bacteria.The European physical journal. E, Soft matter · 2013Article
- Rhodanese functions as sulfur supplier for key enzymes in sulfur energy metabolism.The Journal of biological chemistry · 2012Article
- Heme-copper terminal oxidase using both cytochrome c and ubiquinol as electron donors.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- The elusive third subunit IIa of the bacterial B-type oxidases: the enzyme from the hyperthermophile Aquifex aeolicus.PloS one · 2011Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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 (H(2)S) to molecular oxygen. H(2)S 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 bc(1) complex (complex III), one cytochrome c oxidase (complex IV), and one or two sulfide quinone reductases as well as traces of the monoheme cytochrome c(555) and quinone molecules. In addition, this work strongly suggests that the cytochrome c oxidase in the supercomplex is a ba(3)-type enzyme. The supercomplex has a molecular mass of about 350 kDa and is enzymatically functional, reducing O(2) in the presence of the electron donor, H(2)S. This is the first demonstration of the existence of such a respirasome carrying a sulfide oxidase-oxygen reductase activity. Moreover, the kinetic properties of the sulfide quinone reductase change slightly when integrated in the supercomplex, compared with the free enzyme. We previously purified a complete respirasome involved in hydrogen oxidation and sulfur reduction from Aquifex aeolicus. Thus, two different bioenergetic pathways (sulfur reduction and sulfur oxidation) are organized in this bacterium as supramolecular structures in the membrane. A model for the energetic sulfur metabolism of Aquifex aeolicus is proposed.
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