TY - JOUR
T1 - Generation of Proton‐Motive Force by an archaeal terminal quinol oxidase from Sulfolobus acidocaldarius
AU - Gleissner, Michael
AU - Elferink, Marieke G.L.
AU - Driessen, Arnold J.M.
AU - Konings, Wil N.
AU - Anemüller, Stefan
AU - Schäfer, Günter
N1 - Copyright:
Copyright 2016 Elsevier B.V., All rights reserved.
PY - 1994/9
Y1 - 1994/9
N2 - The terminal quinol oxidase of the cytochrome aa3 type was isolated from the extreme thermo‐acidophilic archaeon Sulfolobus acidocaldarius. In micellar solution, the enzyme oxidized various quinols and exerted the highest activity with the physiological substrate caldariella quinol. The enzyme was functionally reconstituted into monolayer liposomes composed of archaeal tetraether lipids also derived from S. acidocaldarius. With the electron donor system ascorbate and N,N,N′,N′‐tetramethyl‐p‐phenylenediamine, the reconstituted enzyme was more active in the archaeal lipids as compared to lipids derived from Escherichia coli at temperatures above 50°C. Due to the low proton permeability of the tetraether lipids, it was possible to generate a steady‐state transmembrane electrical potential (ΔΨ, interior negative), and transmembrane pH gradient (ΔpH, interior alkaline) at temperatures up to 70°C. The successful functional reconstitution of the cytochrome aa3‐type quinol oxidase from Sulfolobus identifies it as the key energy converter in the respiratory system of this hyperthermophilic archaeon.
AB - The terminal quinol oxidase of the cytochrome aa3 type was isolated from the extreme thermo‐acidophilic archaeon Sulfolobus acidocaldarius. In micellar solution, the enzyme oxidized various quinols and exerted the highest activity with the physiological substrate caldariella quinol. The enzyme was functionally reconstituted into monolayer liposomes composed of archaeal tetraether lipids also derived from S. acidocaldarius. With the electron donor system ascorbate and N,N,N′,N′‐tetramethyl‐p‐phenylenediamine, the reconstituted enzyme was more active in the archaeal lipids as compared to lipids derived from Escherichia coli at temperatures above 50°C. Due to the low proton permeability of the tetraether lipids, it was possible to generate a steady‐state transmembrane electrical potential (ΔΨ, interior negative), and transmembrane pH gradient (ΔpH, interior alkaline) at temperatures up to 70°C. The successful functional reconstitution of the cytochrome aa3‐type quinol oxidase from Sulfolobus identifies it as the key energy converter in the respiratory system of this hyperthermophilic archaeon.
UR - http://www.scopus.com/inward/record.url?scp=0027981410&partnerID=8YFLogxK
U2 - 10.1111/j.1432-1033.1994.00983.x
DO - 10.1111/j.1432-1033.1994.00983.x
M3 - Journal articles
C2 - 7925423
AN - SCOPUS:0027981410
SN - 0014-2956
VL - 224
SP - 983
EP - 990
JO - European Journal of Biochemistry
JF - European Journal of Biochemistry
IS - 3
ER -