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 f
heme bp
heme bn
chlorophyll a
heme x
TDS
Cytochrome b(6)f
PDB: 1VF5
Electron transfer
Proton transport
lumen (p) side
stromal (n) side
e-
to plastocyanin or cytochrome c 6
28.7 Å
29.1 Å
20.4 Å
β-carotene
TDS = tridecylstigmatellin
PQ = plastoquinone
PQH 2 = plastoquinol
PQH 2
2H+
PQ
2Fe-2S
CYTOCHROME b(6)f: A GREEN PLANT CYTOCHROME 385