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 language||English (US)|
|Number of pages||6|
|Journal||Proceedings of the National Academy of Sciences of the United States of America|
|Publication status||Published - Aug 17 1999|
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