Electron transfer in the heliobacterial reaction center: evidence against a quinone-type electron acceptor functioning analogous to A1 in photosystem I.
Membrane fragments from Heliobacillus mobilis were characterized using time resolved optical spectroscopy and photovoltage measurements in order to detect a possible participation of menaquinone (MQ), functioning analogous to the phylloquinone A1 in photosystem I, as intermediate in electron transfer from the primary acceptor A0 to the iron-sulfur cluster FX in the photosynthetic reaction center. The spectroscopic data obtained exclude that electron transfer from a semiquinone anion MQ- to FX occurred in the time window from 2 ns to 4 micros, where it would be expected in analogy to photosystem I. In the case of a prereduction of FX, only the primary pair P798+A0- was formed. The photovoltage data yielded a single kinetic phase with a time constant of 700 ps for the transmembrane electron transfer beyond A0; the relative amplitude of this phase suggests that it reflects electron transfer from A0- to FX.
Brettel
K
K
Section de Bioénergétique, DBCM, CEA and CNRS URA 2096, Centre d'Etudes de Saclay, 91191 Gif-sur-Yvette Cedex, France. brettel@dsvidf.cea.fr
Leibl
W
W
Liebl
U
U
D001419:Bacteria / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D004579:Electron Transport; D045322:Photosynthetic Reaction Center Complex Proteins / Q000378:metabolism*; D014812:Vitamin K / Q000378:metabolism
D045322:Photosynthetic Reaction Center Complex Proteins; D014812:Vitamin K