Quinone reduction by Rhodothermus marinus succinate:menaquinone oxidoreductase is not stimulated by the membrane potential.
Succinate:quinone oxidoreductase (SQR), a di-haem enzyme purified from Rhodothermus marinus, reveals an HQNO-sensitive succinate:quinone oxidoreductase activity with several menaquinone analogues as electron acceptors that decreases with lowering the redox midpoint potential of the quinones. A turnover with the low-potential 2,3-dimethyl-1,4-naphthoquinone that is the closest analogue of menaquinone, although low, can be detected in liposome-reconstituted SQR. Reduction of the quinone is not stimulated by an imposed K+-diffusion membrane potential of a physiological sign (positive inside the vesicles). Nor does the imposed membrane potential increase the reduction level of the haems in R. marinus SQR poised with the succinate/fumarate redox couple. The data do not support a widely discussed hypothesis on the electrogenic transmembrane electron transfer from succinate to menaquinone catalysed by di-haem SQRs. The role of the membrane potential in regulation of the SQR activity is discussed.
Fernandes
Andreia S
AS
Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. da República, Apartado 127, 2784-505 Oeiras, Portugal.
Konstantinov
Alexander A
AA
Teixeira
Miguel
M
Pereira
Manuela M
MM
D016227:Benzoquinones / Q000378:metabolism*; D008081:Liposomes; D008564:Membrane Potentials; D045245:Rhodothermus / Q000201:enzymology*; D013385:Succinate Dehydrogenase / Q000378:metabolism*
D016227:Benzoquinones; D008081:Liposomes; C004532:quinone; D013385:Succinate Dehydrogenase