Generation of proton-motive force by an archaeal terminal quinol oxidase from Sulfolobus acidocaldarius.
The terminal quinol oxidase of the cytochrome aa3 type was isolated from the extreme thermoacidophilic 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 degrees C. Due to the low proton permeability of the tetraether lipids, it was possible to generate a steady-state transmembrane electrical potential (delta psi, interior negative), and transmembrane pH gradient (delta pH, interior alkaline) at temperatures up to 70 degrees 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.
Gleissner
M
M
Institute of Biochemistry, Medical University of Lübeck, Germany.
Elferink
M G
MG
Driessen
A J
AJ
Konings
W N
WN
Anemüller
S
S
Schäfer
G
G
D002384:Catalysis; D003902:Detergents; D004563:Electrochemistry; D003576:Electron Transport Complex IV / Q000737:chemistry; D005614:Freeze Fracturing; D008854:Microscopy, Electron; D010088:Oxidoreductases / Q000737:chemistry*; D011522:Protons; D016945:Sulfolobus acidocaldarius / Q000201:enzymology* / Q000648:ultrastructure
D003902:Detergents; D011522:Protons; D010088:Oxidoreductases; C020094:duroquinol oxidase; D003576:Electron Transport Complex IV