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A cytochrome c containing nitrate reductase plays a role in electron transport for denitrification in Thermus thermophilus without involvement of the bc respiratory complex
CBM ‘Severo Ochoa’ CSIC-UAM, Madrid, Spain.
CBM ‘Severo Ochoa’ CSIC-UAM, Madrid, Spain.
CBM ‘Severo Ochoa’ CSIC-UAM, Madrid, Spain.
2008 (English)In: Molecular Microbiology, ISSN 0950-382X, E-ISSN 1365-2958, Vol. 70, no 2, 507-518 p.Article in journal (Refereed) Published
Abstract [en]

The bc(1) respiratory complex III constitutes a key energy-conserving respiratory electron transporter between complex I (type I NADH dehydrogenase) and II (succinate dehydrogenase) and the final nitrogen oxide reductases (Nir, Nor and Nos) in most denitrifying bacteria. However, we show that the expression of complex III from Thermus thermophilus is repressed under denitrification, and that its role as electron transporter is replaced by an unusual nitrate reductase (Nar) that contains a periplasmic cytochrome c (NarC). Several lines of evidence support this conclusion: (i) nitrite and NO are as effective signals as nitrate for the induction of Nar; (ii) narC mutants are defective in anaerobic growth with nitrite, NO and N2O; (iii) such mutants present decreased NADH oxidation coupled to these electron acceptors; and (iv) complementation assays of the mutants reveal that the membrane-distal heme c of NarC was necessary for anaerobic growth with nitrite, whereas the membrane-proximal heme c was not. Finally, we show evidence to support that Nrc, the main NADH oxidative activity in denitrification, interacts with Nar through their respective membrane subunits. Thus, we propose the existence of a Nrc-Nar respiratory super-complex that is required for the development of the whole denitrification pathway in T. thermophilus.

Place, publisher, year, edition, pages
2008. Vol. 70, no 2, 507-518 p.
National Category
Biochemistry and Molecular Biology Microbiology
URN: urn:nbn:se:umu:diva-81865DOI: 10.1111/j.1365-2958.2008.06429.xISI: 000259526100018PubMedID: 18761683OAI: diva2:658615
Available from: 2013-10-22 Created: 2013-10-22 Last updated: 2013-10-28Bibliographically approved

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