NDLI: Redox-linked transient deprotonation at the binuclear site in the aa 3-type quinol oxidase from Acidianus ambivalens: Implications for proton translocation

Content Provider	PubMed Central
Author	Das, Tapan Kanti Gomes, Cláudio M. Teixeira, Miguel Rousseau, Denis L.
Copyright Year	1999
Abstract	The hyperthermophilic archaeon Acidianus ambivalens expresses a membrane-bound aa 3-type quinol oxidase, when grown aerobically, that we have studied by resonance Raman spectroscopy. The purified aa 3 oxidase, which does not contain bound quinol, undergoes a reversible slow conformational change at heme a 3 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 a 3 formyl group is postulated.
Starting Page	9591
File Format	PDF
ISSN	10916490
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	17
Volume Number	96
Language	English
Publisher	The National Academy of Sciences
Publisher Date	1999-08-17
Access Restriction	Open
Rights Holder	The National Academy of Sciences
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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