TY - JOUR
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, D. 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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U2 - 10.1073/pnas.96.17.9591
DO - 10.1073/pnas.96.17.9591
M3 - Article
C2 - 10449737
AN - SCOPUS:0033578373
SN - 0027-8424
VL - 96
SP - 9591
EP - 9596
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 17
ER -