The following description of the electron transfer – proton transport scheme
is illustrated in Figure 7.26. First, an electron is transferred from doubly
reduced dihydroplastoquinone (PQH 2 ) to a high potential electron transfer
chain that consists of the Reiske iron – sulfur protein and the cytochrome
protein containing heme f. Rappaport, Lavergne and co - workers have reported
a midpoint potential at pH 7.0 of +355 mV for heme f.^76 These two centers
reside on the electropositive (lumen or p) side of the membrane, exterior to
the membrane. As a result, two protons are transferred to the aqueous lumen
phase. A second electron is transferred from PQH 2 sequentially to heme b p ,
Figure 7.26 Electron transfer and proton transport in cytochrome b(6)f: cofactors
(PDB: 1VF5). Visualized using The PyMOL Molecular Graphics System and
ChemDraw Ultra, version 10.0. (Printed with permission of Delano Scientifi c, LLC
and CambridgeSoft Corporation.) (See color plate)
H+e-e- e-e-heme fheme bpheme bnchlorophyll aheme xTDSCytochrome b(6)f
PDB: 1VF5
Electron transfer
Proton transportlumen (p) sidestromal (n) sidee-
to plastocyanin or cytochrome c 628.7 Å29.1 Å20.4 Åβ-caroteneTDS = tridecylstigmatellin
PQ = plastoquinone
PQH 2 = plastoquinolPQH 22H+PQ2Fe-2SCYTOCHROME b(6)f: A GREEN PLANT CYTOCHROME 385