Redox-linked transient deprotonation at the binuclear site in the aa3- type quinol oxidase from Acidianus ambivalens: Implications for proton translocation

T. K. Das, C. M. Gomes, M. Teixeira, Denis L. Rousseau

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29 Citations (Scopus)

Abstract

The hyperthermophilic archaeon Acidianus ambivalens expresses a membrane-bound aa3-type quinol oxidase, when grown aerobically, that we have studied by resonance Raman spectroscopy. The purified aa3 oxidase, which does not contain bound quinol, undergoes a reversible slow conformational change at heme a3 upon reduction, as indicated by a change in the frequency of its heme formyl stretching mode, from 1,660 cm-1 to 1,667 cm-1. In contrast, upon reduction of the integral membrane enzyme or the purified enzyme preincubated with decylubiquinol, this mode appears at 1,667 cm-1 much more rapidly, suggesting a role of the bound quinol in controlling the redox-linked conformational changes. The shift of the formyl mode to higher frequency is attributed to a loss of hydrogen bonding that is associated with a group having a pka of ≃3.8. Based on these observations, a crucial element for proton translocation involving a redox-linked conformational change near the heme a3 formyl group is postulated.

Original languageEnglish (US)
Pages (from-to)9591-9596
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume96
Issue number17
DOIs
StatePublished - Aug 17 1999

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Acidianus
Hydroquinones
Oxidation-Reduction
Protons
Membranes
Raman Spectrum Analysis
Archaea
Enzymes
Hydrogen Bonding
Heme
Oxidoreductases
heme a
duroquinol oxidase

ASJC Scopus subject areas

  • Genetics
  • General

Cite this

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title = "Redox-linked transient deprotonation at the binuclear site in the aa3- type quinol oxidase from Acidianus ambivalens: Implications for proton translocation",
abstract = "The hyperthermophilic archaeon Acidianus ambivalens expresses a membrane-bound aa3-type quinol oxidase, when grown aerobically, that we have studied by resonance Raman spectroscopy. The purified aa3 oxidase, which does not contain bound quinol, undergoes a reversible slow conformational change at heme a3 upon reduction, as indicated by a change in the frequency of its heme formyl stretching mode, from 1,660 cm-1 to 1,667 cm-1. In contrast, upon reduction of the integral membrane enzyme or the purified enzyme preincubated with decylubiquinol, this mode appears at 1,667 cm-1 much more rapidly, suggesting a role of the bound quinol in controlling the redox-linked conformational changes. The shift of the formyl mode to higher frequency is attributed to a loss of hydrogen bonding that is associated with a group having a pka of ≃3.8. Based on these observations, a crucial element for proton translocation involving a redox-linked conformational change near the heme a3 formyl group is postulated.",
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T1 - Redox-linked transient deprotonation at the binuclear site in the aa3- type quinol oxidase from Acidianus ambivalens

T2 - Implications for proton translocation

AU - Das, T. K.

AU - Gomes, C. M.

AU - Teixeira, M.

AU - Rousseau, Denis L.

PY - 1999/8/17

Y1 - 1999/8/17

N2 - The hyperthermophilic archaeon Acidianus ambivalens expresses a membrane-bound aa3-type quinol oxidase, when grown aerobically, that we have studied by resonance Raman spectroscopy. The purified aa3 oxidase, which does not contain bound quinol, undergoes a reversible slow conformational change at heme a3 upon reduction, as indicated by a change in the frequency of its heme formyl stretching mode, from 1,660 cm-1 to 1,667 cm-1. In contrast, upon reduction of the integral membrane enzyme or the purified enzyme preincubated with decylubiquinol, this mode appears at 1,667 cm-1 much more rapidly, suggesting a role of the bound quinol in controlling the redox-linked conformational changes. The shift of the formyl mode to higher frequency is attributed to a loss of hydrogen bonding that is associated with a group having a pka of ≃3.8. Based on these observations, a crucial element for proton translocation involving a redox-linked conformational change near the heme a3 formyl group is postulated.

AB - The hyperthermophilic archaeon Acidianus ambivalens expresses a membrane-bound aa3-type quinol oxidase, when grown aerobically, that we have studied by resonance Raman spectroscopy. The purified aa3 oxidase, which does not contain bound quinol, undergoes a reversible slow conformational change at heme a3 upon reduction, as indicated by a change in the frequency of its heme formyl stretching mode, from 1,660 cm-1 to 1,667 cm-1. In contrast, upon reduction of the integral membrane enzyme or the purified enzyme preincubated with decylubiquinol, this mode appears at 1,667 cm-1 much more rapidly, suggesting a role of the bound quinol in controlling the redox-linked conformational changes. The shift of the formyl mode to higher frequency is attributed to a loss of hydrogen bonding that is associated with a group having a pka of ≃3.8. Based on these observations, a crucial element for proton translocation involving a redox-linked conformational change near the heme a3 formyl group is postulated.

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