2023
DOI: 10.1016/j.jinorgbio.2023.112341
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The terminal oxidase cytochrome bd-I confers carbon monoxide resistance to Escherichia coli cells

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Cited by 3 publications
(2 citation statements)
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“…For this purpose, an Agilent Cary 60 UV-Vis or a Varian Cary 300 Bio UV-Visible spectrophotometer was used. The amount of oxidase present in each strain was estimated from the dithionite-reduced-minus-ferricyanyde-oxidized difference absorption spectrum of sonicated cells using ∆ε 561-580 of 21 mM −1 cm −1 (bd-I and bd-II) [92] and 16.3 mM −1 cm −1 (bo 3 ) [88].…”
Section: Spectroscopic Measurementsmentioning
confidence: 99%
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“…For this purpose, an Agilent Cary 60 UV-Vis or a Varian Cary 300 Bio UV-Visible spectrophotometer was used. The amount of oxidase present in each strain was estimated from the dithionite-reduced-minus-ferricyanyde-oxidized difference absorption spectrum of sonicated cells using ∆ε 561-580 of 21 mM −1 cm −1 (bd-I and bd-II) [92] and 16.3 mM −1 cm −1 (bo 3 ) [88].…”
Section: Spectroscopic Measurementsmentioning
confidence: 99%
“…Of the three E. coli oxidases, cytochrome bo 3 was shown to be the least sensitive to inhibition by CO if the enzymes were purified and detergent-solubilized [87]. In contrast, according to a recent short report [88], cytochrome bd-I is more resistant to inhibition by CO than cytochrome bd-II and cytochrome bo 3 if CO is added to E. coli cell suspensions, at [O 2 ] = 150 µM. Bayly et al also studied the physiological response of Mycobacterium smegmatis to CO [83].…”
Section: Introductionmentioning
confidence: 97%