Effect of respiratory inhibitors and quinone analogues on the aerobic electron transport system of Eikenella corrodens
Abstract The effects of respiratory inhibitors, quinone analogues and artificial substrates on the membrane-bound electron transport system of the fastidious β-proteobacterium Eikenella corrodens grown under O2-limited conditions were studied. NADH respiration in isolated membrane particles were par...
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2021
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oai:doaj.org-article:88e6674af31a41af88ec4179eec362752021-12-02T17:39:20ZEffect of respiratory inhibitors and quinone analogues on the aerobic electron transport system of Eikenella corrodens10.1038/s41598-021-88388-02045-2322https://doaj.org/article/88e6674af31a41af88ec4179eec362752021-04-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-88388-0https://doaj.org/toc/2045-2322Abstract The effects of respiratory inhibitors, quinone analogues and artificial substrates on the membrane-bound electron transport system of the fastidious β-proteobacterium Eikenella corrodens grown under O2-limited conditions were studied. NADH respiration in isolated membrane particles were partially inhibited by rotenone, dicoumarol, quinacrine, flavone, and capsaicin. A similar response was obtained when succinate oxidation was performed in the presence of thenoyltrifluoroacetone and N,N’-dicyclohexylcarbodiimide. NADH respiration was resistant to site II inhibitors and cyanide, indicating that a percentage of the electrons transported can reach O2 without the bc 1 complex. Succinate respiration was sensitive to myxothiazol, antimycin A and 2-heptyl-4-hydroxyquinoline-N-oxide (HQNO). Juglone, plumbagin and menadione had higher reactivity with NADH dehydrogenase. The membrane particles showed the highest oxidase activities with ascorbate-TCHQ (tetrachlorohydroquinone), TCHQ alone, and NADH-TMPD (N,N,N’,N’-tetramethyl-p-phenylenediamine), and minor activity levels with ascorbate-DCPIP (2,6-dichloro-phenolindophenol) and NADH-DCPIP. The substrates NADH-DCPIP, NADH-TMPD and TCHQ were electron donors to cyanide-sensitive cbb' cytochrome c oxidase. The presence of dissimilatory nitrate reductase in the aerobic respiratory system of E. corrodens ATCC 23834 was demonstrated by first time. Our results indicate that complexes I and II have resistance to their classic inhibitors, that the oxidation of NADH is stimulated by juglone, plumbagin and menadione, and that sensitivity to KCN is stimulated by the substrates TCHQ, NADH-DCPIP and NADH-TMPD.Rubén D. Jaramillo-LancheroPaola Suarez-AlvarezLuis Teheran-SierraNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-9 (2021) |
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Medicine R Science Q Rubén D. Jaramillo-Lanchero Paola Suarez-Alvarez Luis Teheran-Sierra Effect of respiratory inhibitors and quinone analogues on the aerobic electron transport system of Eikenella corrodens |
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Abstract The effects of respiratory inhibitors, quinone analogues and artificial substrates on the membrane-bound electron transport system of the fastidious β-proteobacterium Eikenella corrodens grown under O2-limited conditions were studied. NADH respiration in isolated membrane particles were partially inhibited by rotenone, dicoumarol, quinacrine, flavone, and capsaicin. A similar response was obtained when succinate oxidation was performed in the presence of thenoyltrifluoroacetone and N,N’-dicyclohexylcarbodiimide. NADH respiration was resistant to site II inhibitors and cyanide, indicating that a percentage of the electrons transported can reach O2 without the bc 1 complex. Succinate respiration was sensitive to myxothiazol, antimycin A and 2-heptyl-4-hydroxyquinoline-N-oxide (HQNO). Juglone, plumbagin and menadione had higher reactivity with NADH dehydrogenase. The membrane particles showed the highest oxidase activities with ascorbate-TCHQ (tetrachlorohydroquinone), TCHQ alone, and NADH-TMPD (N,N,N’,N’-tetramethyl-p-phenylenediamine), and minor activity levels with ascorbate-DCPIP (2,6-dichloro-phenolindophenol) and NADH-DCPIP. The substrates NADH-DCPIP, NADH-TMPD and TCHQ were electron donors to cyanide-sensitive cbb' cytochrome c oxidase. The presence of dissimilatory nitrate reductase in the aerobic respiratory system of E. corrodens ATCC 23834 was demonstrated by first time. Our results indicate that complexes I and II have resistance to their classic inhibitors, that the oxidation of NADH is stimulated by juglone, plumbagin and menadione, and that sensitivity to KCN is stimulated by the substrates TCHQ, NADH-DCPIP and NADH-TMPD. |
format |
article |
author |
Rubén D. Jaramillo-Lanchero Paola Suarez-Alvarez Luis Teheran-Sierra |
author_facet |
Rubén D. Jaramillo-Lanchero Paola Suarez-Alvarez Luis Teheran-Sierra |
author_sort |
Rubén D. Jaramillo-Lanchero |
title |
Effect of respiratory inhibitors and quinone analogues on the aerobic electron transport system of Eikenella corrodens |
title_short |
Effect of respiratory inhibitors and quinone analogues on the aerobic electron transport system of Eikenella corrodens |
title_full |
Effect of respiratory inhibitors and quinone analogues on the aerobic electron transport system of Eikenella corrodens |
title_fullStr |
Effect of respiratory inhibitors and quinone analogues on the aerobic electron transport system of Eikenella corrodens |
title_full_unstemmed |
Effect of respiratory inhibitors and quinone analogues on the aerobic electron transport system of Eikenella corrodens |
title_sort |
effect of respiratory inhibitors and quinone analogues on the aerobic electron transport system of eikenella corrodens |
publisher |
Nature Portfolio |
publishDate |
2021 |
url |
https://doaj.org/article/88e6674af31a41af88ec4179eec36275 |
work_keys_str_mv |
AT rubendjaramillolanchero effectofrespiratoryinhibitorsandquinoneanaloguesontheaerobicelectrontransportsystemofeikenellacorrodens AT paolasuarezalvarez effectofrespiratoryinhibitorsandquinoneanaloguesontheaerobicelectrontransportsystemofeikenellacorrodens AT luisteheransierra effectofrespiratoryinhibitorsandquinoneanaloguesontheaerobicelectrontransportsystemofeikenellacorrodens |
_version_ |
1718379834038550528 |