Difference between revisions of "Nastasi 2023 J Inorg Biochem"

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Nastasi MR, Borisov VB, Forte E (2023) The terminal oxidase cytochrome bd-I confers carbon monoxide resistance to Escherichia coli cells. https://doi.org/10.1016/j.jinorgbio.2023.112341

» J Inorg Biochem 247:112341. PMID: 37515940 Open Access

Nastasi Martina R, Borisov Vitaliy B, Forte Elena (2023) J Inorg Biochem

Abstract: Carbon monoxide (CO) plays a multifaceted role in the physiology of organisms, from poison to signaling molecule. Heme proteins, including terminal oxidases, are plausible CO targets. Three quinol oxidases terminate the branched aerobic respiratory chain of Escherichia coli. These are the heme‑copper cytochrome bo₃ and two copper-lacking bd-type cytochromes, bd-I and bd-II. All three enzymes generate a proton motive force during the four-electron oxygen reduction reaction that is used for ATP production. The bd-type oxidases also contribute to mechanisms of bacterial defense against various types of stresses. Here we report that in E. coli cells, at the enzyme concentrations tested, cytochrome bd-I is much more resistant to inhibition by CO than cytochrome bd-II and cytochrome bo₃. The apparent half-maximal inhibitory concentration values, IC50, for inhibition of O₂ consumption of the membrane-bound bd-II and bo₃ oxidases by CO at ~150 μM O₂ were estimated to be 187.1 ± 11.1 and 183.3 ± 13.5 μM CO, respectively. Under the same conditions, the maximum inhibition observed with the membrane-bound cytochrome bd-I was 20 ± 10% at ~200 μM CO. • Keywords: Carbon monoxide, Cytochrome, Heme protein, Inhibition, Resistance, Terminal oxidase • Bioblast editor: Plangger M

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2023-08

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 |title=Nastasi MR, Borisov VB, Forte E (2023) The terminal oxidase cytochrome bd-I confers carbon monoxide resistance to Escherichia coli cells. https://doi.org/10.1016/j.jinorgbio.2023.112341
 |info=J Inorg Biochem 247:112341. [https://www.ncbi.nlm.nih.gov/pubmed/37515940 PMID: 37515940 Open Access]
-|authors=Nastasi MR, Borisov VB, Forte E
+|authors=Nastasi Martina R, Borisov Vitaliy B, Forte Elena
 |year=2023
 |journal=J Inorg Biochem
-|abstract=Carbon monoxide (CO) plays a multifaceted role in the physiology of organisms, from poison to signaling molecule. Heme proteins, including terminal oxidases, are plausible CO targets. Three quinol oxidases terminate the branched aerobic respiratory chain of Escherichia coli. These are the heme‑copper cytochrome bo3 and two copper-lacking bd-type cytochromes, bd-I and bd-II. All three enzymes generate a proton motive force during the four-electron oxygen reduction reaction that is used for ATP production. The bd-type oxidases also contribute to mechanisms of bacterial defense against various types of stresses. Here we report that in E. coli cells, at the enzyme concentrations tested, cytochrome bd-I is much more resistant to inhibition by CO than cytochrome bd-II and cytochrome bo3. The apparent half-maximal inhibitory concentration values, IC50, for inhibition of O2 consumption of the membrane-bound bd-II and bo3 oxidases by CO at ~150 μM O2 were estimated to be 187.1 ± 11.1 and 183.3 ± 13.5 μM CO, respectively. Under the same conditions, the maximum inhibition observed with the membrane-bound cytochrome bd-I was 20 ± 10% at ~200 μM CO.
+|abstract=Carbon monoxide (CO) plays a multifaceted role in the physiology of organisms, from poison to signaling molecule. Heme proteins, including terminal oxidases, are plausible CO targets. Three quinol oxidases terminate the branched aerobic respiratory chain of ''Escherichia coli''. These are the heme‑copper cytochrome bo<sub>3</sub> and two copper-lacking bd-type cytochromes, bd-I and bd-II. All three enzymes generate a proton motive force during the four-electron oxygen reduction reaction that is used for ATP production. The bd-type oxidases also contribute to mechanisms of bacterial defense against various types of stresses. Here we report that in ''E. coli cells'', at the enzyme concentrations tested, cytochrome bd-I is much more resistant to inhibition by CO than cytochrome bd-II and cytochrome bo<sub>3</sub>. The apparent half-maximal inhibitory concentration values, IC50, for inhibition of O<sub>2</sub> consumption of the membrane-bound bd-II and bo<sub>3</sub> oxidases by CO at ~150 μM O<sub>2</sub> were estimated to be 187.1 ± 11.1 and 183.3 ± 13.5 μM CO, respectively. Under the same conditions, the maximum inhibition observed with the membrane-bound cytochrome bd-I was 20 ± 10% at ~200 μM CO.
+|keywords=Carbon monoxide, Cytochrome, Heme protein, Inhibition, Resistance, Terminal oxidase
 |editor=[[Plangger M]]
 }}