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Volume 159, Issue Pt_12

Membrane-bound oxygen reductases of the anaerobic sulfate-reducing Hildenborough: roles in oxygen defence and electron link with periplasmic hydrogen oxidation Free

Abstract

Cytoplasmic membranes of the strictly anaerobic sulfate-reducing bacterium Hildenborough contain two terminal oxygen reductases, a quinol oxidase and a cytochrome oxidase (). Viability assays pointed out that single Δ Δ and double ΔΔ deletion mutant strains were more sensitive to oxygen exposure than the WT strain, showing the involvement of these oxygen reductases in the detoxification of oxygen. The Δ strain was slightly more sensitive than the Δ strain, pointing to the importance of the cytochrome oxidase in oxygen protection. Decreased O reduction rates were measured in mutant cells and membranes using lactate, NADH, ubiquinol and menadiol as substrates. The affinity for oxygen measured with the quinol oxidase ( , 300 nM) was higher than that of the cytochrome oxidase ( , 620 nM). The total membrane activity of the quinol oxidase was higher than that of the cytochrome oxidase activity in line with the higher expression of the oxidase genes. In addition, analysis of the ΔΔ mutant strain indicated the presence of at least one O-scavenging membrane-bound system able to reduce O with menaquinol as electron donor with an O affinity that was two orders of magnitude lower than that of the quinol oxidase. The lower O reductase activity in mutant cells with hydrogen as electron donor and the use of specific inhibitors indicated an electron transfer link between periplasmic H oxidation and membrane-bound oxygen reduction via the menaquinol pool. This linkage is crucial in defence of the strictly anaerobic bacterium against oxygen stress.

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2013-12-01
2024-04-16
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Membrane-bound oxygen reductases of the anaerobic sulfate-reducing Desulfovibrio vulgaris Hildenborough: roles in oxygen defence and electron link with periplasmic hydrogen oxidation
Microbiology 159, 2663 (2013); https://doi.org/10.1099/mic.0.071282-0
/content/journal/micro/10.1099/mic.0.071282-0
/content/journal/micro/10.1099/mic.0.071282-0
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