The cytochrome b6f
complex (plastoquinol—plastocyanin
reductase;
EC
1.10.99.1) of
chloroplasts and
cyanobacteria transfers
electrons between the two reaction
center complexes of oxygenic
photosynthetic membranes,
photosystem I and photosystem
II, and participates in formation
of the transmembrane
electrochemical
proton gradient by also
transferring protons from the
stromal to the internal lumen
compartment. It is minimally
composed of four subunits:
cytochrome b6,
carrying a low- and a
high-potential heme groups (bL
and bH);
cytochrome f
with one covalently bound heme
c;
Rieske iron-sulfur protein
(ISP) containing a single [Fe2S2]
cluster; and subunit IV (17
kDa protein). In its structure and
functions, the cytochrome b6f
complex bears extensive analogy to
the
cytochrome bc1
complex of
mitochondria and
photosynthetic
purple bacteria. However,
there are important differences
between the two complexes:
The single-polypeptide
cytochrome b in the
cytochrome bc1
complex corresponds to
cytochrome b6
and subunit IV in the cytochrome
b6f
complex
Cytochrome f and
cytochrome c1
are not homologous
The cytochrome b6f
complex contains additional
chromophores,
chlorophyll a,
β-carotene and atypical heme
ci (heme x),
the latter being linked by a
single thioether bond to
cytochrome b6
The cytochrome b6f
complex is responsible for
"non-cyclic" (1) and
"cyclic" (2) electron
transfer between two mobile redox
carriers,
plastoquinol (QH2)
and plastocyanin:
H2O
→
photosystem II
→
QH2
→
Cyt b6f
→
plastocyanin
→
photosystem I
→
NADP+
(1)
QH2
→
Cyt b6f
→
plastocyanin
→
photosystem I
→
Q
(2)
Electron transfer is coupled
with the translocation of protons
across the membrane, thus
generating proton-motive force in
the form of an electrochemical
proton potential which can drive
ATP synthesis. The crystal
structure of cytochrome b6f
complexes from Chlamydomonas
reinhardtii and
Mastigocladus laminosus have
been determined.
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