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Information on EC 7.1.1.6 - plastoquinol-plastocyanin reductase
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EC Tree
7.1.1.6 plastoquinol-plastocyanin reductaseIUBMB Comments
Contains two b-type cytochromes, two c-type cytochromes (cn and f), and a [2Fe-2S] Rieske cluster. The enzyme plays a key role in photosynthesis, transferring electrons from photosystem II (EC 1.10.3.9) to photosystem I (EC 1.97.1.12). Cytochrome c-552 can act as acceptor instead of plastocyanin, but more slowly. In chloroplasts, protons are translocated through the thylakoid membrane from the stroma to the lumen. The mechanism occurs through the Q cycle as in EC 7.1.1.8, quinol---cytochrome-c reductase (complex III) and involves electron bifurcation.
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Word Map
- 7.1.1.6
- photosystems
- chloroplast
- thylakoids
- chlorophyll
- chlamydomonas
- heme
- reinhardtii
- spinach
- plastoquinone
- cyanobacterium
-
light-harvesting
- synechocystis
-
antenna
- ubiquinol
- stigmatellin
- lhcii
-
supercomplexes
-
risps
-
q-cycle
- 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone
-
nucleus-encoded
-
chromatophore
-
grana
-
dbmib
-
p-side
-
photoinhibition
-
photoprotection
- myxothiazol
-
extramembrane
-
apocytochrome
- laminosus
-
nonphotochemical
-
intersystem
-
mastigocladus
-
rieske-type
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
rieske iron-sulfur protein, cytochrome b6f complex, cytochrome b(6)f complex, cytochrome b6f, cytochrome b6/f complex, rieske fe-s protein, cytochrome b6-f complex, cytochrome b6 f complex, cyt b6f complex, rieske [2fe-2s] protein, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Cyt b6 f
Cyt b6f complex
cytochrome b6 f complex
cytochrome b6-f complex
-
-
-
-
cytochrome b6/f complex
cytochrome b6f
cytochrome b6f /Rieske Fe-S protein
cytochrome b6f complex
EC 1.10.9.1
-
-
formerly
-
EC 1.10.99.1
-
-
formerly
-
plastoquinol/plastocyanin oxidoreductase
-
-
-
-
plastoquinol:plastocyanin/cytochrome c6 oxidoreductase
quinol:plastocyanin oxidoreductase
reductase, plastoquinol-plastocyanin
-
-
-
-
Rieske iron-sulfur protein
RISP
cytochrome b6/f complex
-
-
-
-
Rieske iron-sulfur protein
-
-
-
-
RISP
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
plastoquinol + 2 oxidized plastocyanin + 2 H+[side 1] = plastoquinone + 2 reduced plastocyanin + 4 H+[side 2]
plastoquinol + 2 oxidized plastocyanin + 2 H+[side 1] = plastoquinone + 2 reduced plastocyanin + 4 H+[side 2]
mechanism
-
plastoquinol + 2 oxidized plastocyanin + 2 H+[side 1] = plastoquinone + 2 reduced plastocyanin + 4 H+[side 2]
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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SYSTEMATIC NAME
IUBMB Comments
plastoquinol:oxidized-plastocyanin oxidoreductase
Contains two b-type cytochromes, two c-type cytochromes (cn and f), and a [2Fe-2S] Rieske cluster. The enzyme plays a key role in photosynthesis, transferring electrons from photosystem II (EC 1.10.3.9) to photosystem I (EC 1.97.1.12). Cytochrome c-552 can act as acceptor instead of plastocyanin, but more slowly. In chloroplasts, protons are translocated through the thylakoid membrane from the stroma to the lumen. The mechanism occurs through the Q cycle as in EC 7.1.1.8, quinol---cytochrome-c reductase (complex III) and involves electron bifurcation.
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CAS REGISTRY NUMBER
COMMENTARY
79079-13-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,3-dimethyl-6-geranyl-1,4-benzoquinol + 3-chloro-5-hydroxyl-2-methyl-6-decyl-1,4-benzoquinone + H+ [side 1]
2,3-dimethyl-6-geranyl-1,4-benzoquinone + 3-chloro-5-hydroxyl-2-methyl-6-decyl-1,4-benzoquinol + H+[side 2]
-
-
-
-
?
plastoquinol + 2 oxidized plastocyanin
plastoquinone + 2 reduced plastocyanin
-
-
-
-
?
plastoquinol + 2 oxidized plastocyanin + 2 H+[side 1]
plastoquinone + 2 reduced plastocyanin + 2 H+[side 2]
-
-
-
-
?
plastoquinol + cytochrome c1
plastoquinone + reduced cytochrome c1
-
-
-
-
?
plastoquinol + cytochrome c6
plastoquinone + reduced cytochrome c6
-
-
-
-
?
plastoquinol + oxidized plastocyanin + H+[side 1]
plastoquinone + reduced plastocyanin + H+[side 2]
plastoquinol-1 + oxidized plastocyanin + H+[side 1]
plastoquinone-1 + reduced plastocyanin + H+[side 2]
-
-
-
-
?
duroquinol + plastocyanin
duroquinone + reduced plastocyanin
-
-
-
-
?
plastoquinol + cytochrome f
plastoquinone + reduced cytochrome f
-
-
-
-
?
plastoquinol + cytochrome f
plastoquinone + reduced cytochrome f
-
-
-
-
?
plastoquinol + oxidized plastocyanin + H+[side 1]
plastoquinone + reduced plastocyanin + H+[side 2]
-
-
-
-
?
plastoquinol + oxidized plastocyanin + H+[side 1]
plastoquinone + reduced plastocyanin + H+[side 2]
-
-
-
?
plastoquinol + plastocyanin
plastoquinone + reduced plastocyanin
-
-
-
-
?
plastoquinol + plastocyanin
plastoquinone + reduced plastocyanin
-
-
-
-
?
plastoquinol + plastocyanin
plastoquinone + reduced plastocyanin
-
-
-
-
?
plastoquinol + plastocyanin
plastoquinone + reduced plastocyanin
-
Q-cycle, electron transfer in photosynthesis, cytochrome f is not an obligatory intermediate for electrons flowing though the cytochrome b6/f complex
-
-
?
plastoquinol + plastocyanin
plastoquinone + reduced plastocyanin
Cyanobacterium sp.
-
-
-
-
?
plastoquinol + plastocyanin
plastoquinone + reduced plastocyanin
Lactuca sp.
-
best electron donor is decylplastoquinol
-
-
?
plastoquinol + plastocyanin
plastoquinone + reduced plastocyanin
Lactuca sp.
-
best electron acceptor: ferricyanide
-
-
?
plastoquinol + plastocyanin
plastoquinone + reduced plastocyanin
-
-
-
-
?
plastoquinol + plastocyanin
plastoquinone + reduced plastocyanin
-
-
-
-
?
plastoquinol + plastocyanin
plastoquinone + reduced plastocyanin
-
enzyme also reduces algal cytochrome c
-
-
?
plastoquinol + plastocyanin
plastoquinone + reduced plastocyanin
-
-
-
-
?
plastoquinol + plastocyanin
plastoquinone + reduced plastocyanin
-
best electron acceptors: plastocyanin from Anabaena variabilis, cytochrome c-553 from Anabaena variabilis, cytochrome c from horse heart
-
-
?
plastoquinol + plastocyanin
plastoquinone + reduced plastocyanin
-
best electron donor: plastoquinol-9
-
-
?
additional information
?
-
-
a pathway of cytochrome c biogenesis is involved in the assembly of the cytochrome b6f complex in Arabidopsis chloroplasts
-
-
?
additional information
?
-
-
under white-light illumination and aerobic conditions, chlorophyll a bound in the intact Cyt b6f can be bleached by light-induced singlet oxygen. Under similar experimental conditions, singlet oxygen is also detected in the Rieske-depleted Cyt b6f complex, but not in the isolated Rieske FeS protein
-
-
?
additional information
?
-
-
photosystem I and II are reaction centers that capture light energy in order to drive oxygenic photosynthesis. They can only do so by interacting with multisubunit cytochrome b6f complex. This complex receives electrons from photosystem II and passes them to phosptosystem I, pumping protons across the membrane and powering the Q-cycle. Cytochrome b6f can switch to a cyclic mode of electron transfer around photosystem I using an unknown pathway
-
-
?
additional information
?
-
detectable conformational changes in the ISP binding site of cyt b6 f in presence of dioleoylphosphatidylglycerol and dioleoylphosphatidylcholine
-
-
?
additional information
?
-
-
proton translocation with b6-f complex incorporated into liposomes
-
-
?
additional information
?
-
-
proton translocation with b6-f complex incorporated into liposomes
-
-
?
additional information
?
-
-
proton translocation with b6-f complex incorporated into liposomes
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
plastoquinol + 2 oxidized plastocyanin + 2 H+[side 1]
plastoquinone + 2 reduced plastocyanin + 2 H+[side 2]
-
-
-
-
?
plastoquinol + cytochrome c6
plastoquinone + reduced cytochrome c6
-
-
-
-
?
plastoquinol + oxidized plastocyanin + H+[side 1]
plastoquinone + reduced plastocyanin + H+[side 2]
plastoquinol + oxidized plastocyanin + H+[side 1]
plastoquinone + reduced plastocyanin + H+[side 2]
-
-
-
-
?
plastoquinol + oxidized plastocyanin + H+[side 1]
plastoquinone + reduced plastocyanin + H+[side 2]
-
-
-
?
plastoquinol + plastocyanin
plastoquinone + reduced plastocyanin
-
-
-
-
?
plastoquinol + plastocyanin
plastoquinone + reduced plastocyanin
-
Q-cycle, electron transfer in photosynthesis, cytochrome f is not an obligatory intermediate for electrons flowing though the cytochrome b6/f complex
-
-
?
additional information
?
-
-
a pathway of cytochrome c biogenesis is involved in the assembly of the cytochrome b6f complex in Arabidopsis chloroplasts
-
-
?
additional information
?
-
-
photosystem I and II are reaction centers that capture light energy in order to drive oxygenic photosynthesis. They can only do so by interacting with multisubunit cytochrome b6f complex. This complex receives electrons from photosystem II and passes them to phosptosystem I, pumping protons across the membrane and powering the Q-cycle. Cytochrome b6f can switch to a cyclic mode of electron transfer around photosystem I using an unknown pathway
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heme
-
atypical as it is covalently bound by one thioether linkage and has no axial amino acid ligand
heme
-
cytochrome b6 subunit of the cytochrome b6f complex is a multiheme protein. Two b-type hemes are bound non-covalently to the protein, whereas the third heme (heme cn) is covalently attached via an atypical thioether bond. HCF208, a homolog of Chlamydomonas CCB2, is required for accumulation of native cytochrome b6 in Arabidopsis thaliana
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2Fe-2S
Fe
Fe2+
Rieske iron-sulfur protein, ISP, containing a [2Fe-2S] cluster, conformational flexibility of the cyt b6 f ISP subunit
Iron
-
PetC1 is the major Rieske iron-sulfur protein in the cytochrome b6f complex. PetC2 can partly replace the dominating Rieske isoform PetC1, PetC3 is unable to functionally replace either PetC1 or PetC2 and may have a special function involving a special donor with a lower redox potential than plastoquinone
Zn2+
-
concurrent action of Zn2+ ions on the re-reduction of cytochrome c1 by the Rieske protein, voltage generation, and proton release from the bc1
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(E)-beta-methoxyacrylate stilbene
-
weak inhibition, retards concurrently the flashinduced re-reduction of cytochrome f, the oxidation of cytochrome b6 and the onset of voltage generation, thereby hardly affecting the rate of the flash-induced cytochrome b6 reduction and the steady turnover of the bf
2-azido-2',2,4'-trinitro-6-sec-butyl-diphenyl ether
-
DNP-ANT, 50% inhibition at 0.00015 mM
2-heptyl-4-hydroxyquinoline N-oxide
-
inhibition at low concentrations, 0.001-0.002 mM
3-Azido-2-methyl-5-methoxy-6-(3,7-dimethyloctyl)-1,4-benzoquinone
-
azido-Q, 45% inhibition at 30 mol inhibitor per 1 mol cytochrome f
2,5-dibromo-3-methyl-6-isopropylbenzoquinone
-
the orientation of the iron sulfur protein is differentially affected by binding of one or two 2,5-dibromo-3-methyl-6-isopropylbenzoquinone molecules in the quinol oxidase pocket
2,5-dibromo-3-methyl-6-isopropylbenzoquinone
-
the orientation of the iron sulfur protein is differentially affected by binding of one or two 2,5-dibromo-3-methyl-6-isopropylbenzoquinone molecules in the quinol oxidase pocket
2,5-dibromo-3-methyl-6-isopropylbenzoquinone
-
DBMIB or dibromothymoquinone, 75% inhibition at 0.005 mM, reactivation by 3-chloro-5-hydroxyl-2-methyl-6-decyl-1,4-benzoquinone
2,5-dibromo-3-methyl-6-isopropylbenzoquinone
-
-
2,5-dibromo-3-methyl-6-isopropylbenzoquinone
-
-
2-Iodo-6-isopropyl-3-methyl-2',2,4'-trinitrodiphenyl ether
-
DNP-INT, inhibits Rieske protein
2-Iodo-6-isopropyl-3-methyl-2',2,4'-trinitrodiphenyl ether
-
50% inhibition at 0.00012 mM
2-n-Nonyl-4-hydroxyquinoline N-oxide
-
weak inhibition, retards concurrently the flashinduced re-reduction of cytochrome f, the oxidation of cytochrome b6 and the onset of voltage generation, thereby hardly affecting the rate of the flash-induced cytochrome b6 reduction and the steady turnover of the bf
5-(n-undecyl)-6-hydroxy-4,7-dioxobenzothiazole
-
inhibition at low concentrations, 0.001-0.002 mM
Stigmatellin
-
inhibits the cytochrome b6/f electrogenic activities by blocking the plastoquinol oxidation site
additional information
-
no inhibition by 0.3 mM decyl-plastoquinone
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-chloro-5-hydroxy-2-methyl-6-decyl-1,4-benzoquinone
-
activation with substrate 2,3-dimethyl-6-geranyl-1,4-benzoquinone
additional information
-
the bf complex, however, can be dark-activated via reduction of heme cn by ferredoxin
-
valinomycin
-
2.3fold stimulation of reconstituted cytochrome complexes, effect can be enhanced by addition of nigericin
valinomycin
-
2.3fold stimulation of reconstituted cytochrome complexes, effect can be enhanced by addition of nigericin
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Anemia
The mitochondrial respiratory chain is essential for haematopoietic stem cell function.
Asthma
Overview on Interactive Role of Inflammation, Reactive Oxygen Species, and Calcium Signaling in Asthma, COPD, and Pulmonary Hypertension.
Dehydration
Photoprotection conferred by changes in photosynthetic protein levels and organization during dehydration of a homoiochlorophyllous resurrection plant.
Dehydration
Protection of the photosynthetic apparatus against dehydration stress in the resurrection plant Craterostigma pumilum.
Hypersensitivity
PGR5-Dependent Cyclic Electron Flow Protects Photosystem I under Fluctuating Light at Donor and Acceptor Sides.
Hypertension, Pulmonary
Mitochondrial Rieske iron-sulfur protein in pulmonary artery smooth muscle: A key primary signaling molecule in pulmonary hypertension.
Hypertension, Pulmonary
Rieske iron-sulfur protein induces FKBP12.6/RyR2 complex remodeling and subsequent pulmonary hypertension through NF-?B/cyclin D1 pathway.
Iron Deficiencies
Effects of iron limitation on the expression of metabolic genes in the marine cyanobacterium Trichodesmium erythraeum IMS101.
Lung Diseases
Overview on Interactive Role of Inflammation, Reactive Oxygen Species, and Calcium Signaling in Asthma, COPD, and Pulmonary Hypertension.
Pulmonary Disease, Chronic Obstructive
Overview on Interactive Role of Inflammation, Reactive Oxygen Species, and Calcium Signaling in Asthma, COPD, and Pulmonary Hypertension.
Starvation
Evidence for a role of ClpP in the degradation of the chloroplast cytochrome b(6)f complex.
Starvation
RESPONSE OF NANNOCHLOROPSIS GADITANA TO NITROGEN STARVATION INCLUDES A DE NOVO BIOSYNTHESIS OF TRIACYLGLYCEROLS, A DECREASE OF CHLOROPLAST GALACTOLIPIDS AND A REORGANIZATION OF THE PHOTOSYNTHETIC APPARATUS.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0032 - 0.0039
2,3-dimethyl-6-geranyl-1,4-benzoquinol
-
depending on presence of activator
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Lactuca sp.
-
turnover number with several plastoquinol analogues
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
14-20 micromol cytochrome c-552 reduced per nmol cytochrome f per h
additional information
-
specific activity after depletion and reconstitution with Rieske protein
additional information
-
specific activity depends on electron donor and acceptor
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
plastid cytochrome b6f-complex iron-sulfur subunit protein
TrEMBL
brenda
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
efficient cytochrome b6f complex biogenesis occurs only in young leaves. The capacity for de novo synthesis of the complex is very low in mature and aging leaves. Ontogenetic down-regulation of cytochrome b6f complex biogenesis occurs at the post-transcriptional level
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
cytochrome b6f is a dimeric protochlorophyll a binding complex in etioplasts
brenda
-
-
brenda
-
the cytochrome b6f complex is located in the appressed granal membranes and nonappressed stroma thylakoids
brenda
-
localization throughout the thylakoid without specialized compartmentation
brenda
-
-
395289, 395292, 395293, 395294, 395295, 395302, 395303, 395305, 395308, 395309, 395313, 395316, 395322, 395324
brenda
-
localized between the appressed and the non-appressed membranes
brenda
-
localization throughout the thylakoid without specialized compartmentation
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
cytochrome bc1-complexes of animals and bacteria, as well as related cytochrome b6 f complexes of plants and cyanobacteria are dimeric quinol:cytochrome c/plastocyanin oxidoreductases capable of translocating protons across energy-converting membranes. These enzymes oxidize two quinolmolecules in their catalytic centers P to yield one quinol molecule in another catalytic center N. The simplest cytochrome bc1-complexes of Rhodobacter capsulatus, which contains only 3 subunits, matches the structure of the three catalytic subunits of mitochondrial bc1
physiological function
additional information
physiological function
-
the membrane-embedded cytochrome b6f complex mediates electron transport between the photosystem II and photosystem I reaction center complexes in oxygenic photosynthesis
physiological function
-
the pigment-protein assembly of the Cyt b6f complex per se is crucial for photo-protection
physiological function
-
the spinach complex contains diaphorase activity diagnostic of the 35 kDa petH polypeptide and is active in facilitating ferredoxin-dependent electron transfer from NADPH to the cytochrome b6f complex
physiological function
-
the spinach complex contains diaphorase activity diagnostic of the 35 kDa petH polypeptide and is active in facilitating ferredoxin-dependent electron transfer from NADPH to the cytochrome b6f complex
physiological function
-
the spinach complex contains diaphorase activity diagnostic of the 35 kDa petH polypeptide and is active in facilitating ferredoxin-dependent electron transfer from NADPH to the cytochrome b6f complex
physiological function
cytochrome b6 f catalyzes quinone redox reactions within photosynthetic membranes to generate a transmembrane proton electrochemical gradient for ATP synthesis. A key step involves the transfer of an electron from the [2Fe-2S] cluster of the iron-sulfur protein extrinsic domain to the cytochrome f heme across a distance of 26 A, which is too large for competent electron transfer but could be bridged by translation-rotation of the iron-sulfur protein
physiological function
-
the subunit IV binds single molecules of chlorophyll alpha and beta-carotene, which are likely to be involved in photoprotection
physiological function
-
two-thirds of the proton gradient used for transmembrane free energy storage in oxygenic photosynthesis is generated by the cytochrome b6f complex
physiological function
-
the spinach complex contains diaphorase activity diagnostic of the 35 kDa petH polypeptide and is active in facilitating ferredoxin-dependent electron transfer from NADPH to the cytochrome b6f complex
-
additional information
-
proton uptake pathway from the electrochemically negative (n) aqueous phase to the n-side quinone binding site of the complex, and a probable route for proton exit to the positive phase resulting from quinol oxidation, overview. The simplest n-side proton pathway extends from the aqueous phase via Asp20 and Arg207 (cytochrome b6 subunit) to quinone bound axially to heme cn. On the positive side, the heme-proximal Glu78 (subunit IV), which accepts protons from plastosemiquinone, defines a route for H+ transfer to the aqueous phase
additional information
-
Q-cycle in the cytochrome bc1 complex using the X-ray structure of the three catalytic subunits of a dimeric bc1 of phototrophic bacteria, i.e. the X-ray structure of the bc1 of Rhodobacter sphaeroides, PDB entry 2QJY, modificationss of Mitchell's Q-cycle, detailed overview
Show AA Sequence and Transmembrane Helices (1572 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
128000
160000
-
calculation from ultraviolet spectrum assuming subunit stoichiometry of 1:2:1:2
17311
-
x * 35313 (subunit FNR) + x * 31934 (cytochrome f) + x * 24886 (cytochrome b) + x * 18935 (subunit PetC) + x * 17311 (subunit PetD) + x * 4197 (subunit PetG) + x * 3971 (subunit PetM) + x * 3477 (subunit PetL) + x * 3197 (subunit PetN), electrospray ionization mass spectrometry
17528
-
x * 32269 (cytochrome f) + x * 24709 (cytochrome b) + x * 19294 (subunit PetC) + x * 17528 (subunit PetD) + x * 4057 (subunit PetG) + x * 3841 (subunit PetM) + x * 3530 (subunit PetL) + x * 3303 (subunit PetN), electrospray ionization mass spectrometry
18935
-
x * 35313 (subunit FNR) + x * 31934 (cytochrome f) + x * 24886 (cytochrome b) + x * 18935 (subunit PetC) + x * 17311 (subunit PetD) + x * 4197 (subunit PetG) + x * 3971 (subunit PetM) + x * 3477 (subunit PetL) + x * 3197 (subunit PetN), electrospray ionization mass spectrometry
19294
-
x * 32269 (cytochrome f) + x * 24709 (cytochrome b) + x * 19294 (subunit PetC) + x * 17528 (subunit PetD) + x * 4057 (subunit PetG) + x * 3841 (subunit PetM) + x * 3530 (subunit PetL) + x * 3303 (subunit PetN), electrospray ionization mass spectrometry
220000
24709
-
x * 32269 (cytochrome f) + x * 24709 (cytochrome b) + x * 19294 (subunit PetC) + x * 17528 (subunit PetD) + x * 4057 (subunit PetG) + x * 3841 (subunit PetM) + x * 3530 (subunit PetL) + x * 3303 (subunit PetN), electrospray ionization mass spectrometry
24886
-
x * 35313 (subunit FNR) + x * 31934 (cytochrome f) + x * 24886 (cytochrome b) + x * 18935 (subunit PetC) + x * 17311 (subunit PetD) + x * 4197 (subunit PetG) + x * 3971 (subunit PetM) + x * 3477 (subunit PetL) + x * 3197 (subunit PetN), electrospray ionization mass spectrometry
310000
-
calculated from the composition of subunits after gel filtration
31934
-
x * 35313 (subunit FNR) + x * 31934 (cytochrome f) + x * 24886 (cytochrome b) + x * 18935 (subunit PetC) + x * 17311 (subunit PetD) + x * 4197 (subunit PetG) + x * 3971 (subunit PetM) + x * 3477 (subunit PetL) + x * 3197 (subunit PetN), electrospray ionization mass spectrometry
32269
-
x * 32269 (cytochrome f) + x * 24709 (cytochrome b) + x * 19294 (subunit PetC) + x * 17528 (subunit PetD) + x * 4057 (subunit PetG) + x * 3841 (subunit PetM) + x * 3530 (subunit PetL) + x * 3303 (subunit PetN), electrospray ionization mass spectrometry
35313
-
x * 35313 (subunit FNR) + x * 31934 (cytochrome f) + x * 24886 (cytochrome b) + x * 18935 (subunit PetC) + x * 17311 (subunit PetD) + x * 4197 (subunit PetG) + x * 3971 (subunit PetM) + x * 3477 (subunit PetL) + x * 3197 (subunit PetN), electrospray ionization mass spectrometry
128000
-
2 * 128000, calculated from composition of subunits after gel filtration
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heterooligomer
additional information
?
-
x * 32269 (cytochrome f) + x * 24709 (cytochrome b) + x * 19294 (subunit PetC) + x * 17528 (subunit PetD) + x * 4057 (subunit PetG) + x * 3841 (subunit PetM) + x * 3530 (subunit PetL) + x * 3303 (subunit PetN), electrospray ionization mass spectrometry
?
-
x * 35313 (subunit FNR) + x * 31934 (cytochrome f) + x * 24886 (cytochrome b) + x * 18935 (subunit PetC) + x * 17311 (subunit PetD) + x * 4197 (subunit PetG) + x * 3971 (subunit PetM) + x * 3477 (subunit PetL) + x * 3197 (subunit PetN), electrospray ionization mass spectrometry
dimer
-
2 * 128000, calculated from composition of subunits after gel filtration
additional information
-
complex consists of polypeptides with the following molecular weights: cytochrome f MW 39500, cytochrome b6 MW 18000, Rieske FeS protein MW 18500, subunit IV MW 12500 and 3 proteins with a MW of 4000 each, SDS-PAGE
additional information
-
complex consists of polypeptides with the following molecular weights: 35000, 23000, 19000, 16000, SDS-PAGE
additional information
-
eight subunit, 220000 Da symmetric dimeric complex
additional information
-
complex consists of polypeptides with the following molecular weights: 37000, 23000, 16000, SDS-PAGE
additional information
-
eight subunit, 220000 Da symmetric dimeric complex, subunits: cytochrome f (32273 Da), cytochrome b6 (24712 Da), Rieske iron-sulfur protein (19295 Da), subunit VI (17528 Da), PetG (4058 Da), PetM (3841 Da), PetL (3530 Da), PetN (3304 Da), determined by electrospray mass spectrometry
additional information
-
subunit PetL is primarily required for proper conformation of the Rieske protein, leading to stability and formation of dimeric Cyt b6 f complexes. PetL is dispensable for photoautotrophic growth, but crucial for accumulation of dimeric Cyt b6 f complexes and photosynthetic redox regulation in tobacco
additional information
-
heterooligomer, subunits: cytochrome f (31769 Da), cytochrome b6 (24757 Da), Rieske iron-sulfur protein (19107 Da (acetylated), 19064 Da), subunit VI (17404 Da), PetG (4023 Da), PetM (3574 Da), PetN (3262 Da), PetL (3253 Da), masses measured by electrospray-ionization MS, purified b6f complex has a dimeric structure
additional information
-
complex consists of the following polypeptides: cytochrome f MW 37300, cytochrome b6 MW 19500, Rieske FeS protein MW 19000, subunit IV MW 15200, SDS-PAGE
additional information
-
complex consists of polypeptides with the following molecular weights: 33000, 23500, 20000, 17000, SDS-PAGE
additional information
-
complex consists of polypeptides with the following molecular weights: 33000, 23500, 20000, 17000, SDS-PAGE
additional information
-
complex consists of polypeptides with the following molecular weights: 34000, 33000, 23500, 20000, 17500, SDS-PAGE
additional information
-
complex consists of polypeptides with the following molecular weights: 34000, 33000, 23000, 20000, 17500, SDS-PAGE
additional information
-
complex consists of the following polypeptides: cytochrome f MW 33000, cytochrome b6 MW 23000, Rieske FeS protein MW 20000, and a polypeptide with the molecular weight of 17000, SDS-PAGE
additional information
-
complex consists of the following polypeptides: cytochrome f MW 33000, cytochrome b563 MW 23500, Rieske FeS protein MW20000, subunit IV MW 17000, SDS-PAGE
additional information
-
complex consists of the following polypeptides: cytochrome f MW 33500 cytochrome b563 MW 22000, Rieske FeS protein MW 19000, subunit IV MW 16500, and a polypeptide with the molecular weight of 37000, SDS-PAGE
additional information
-
complex consists of the following polypeptides: cytochrome f MW 35000, cytochrome b6 MW 20000, Rieske FeS protein MW 18000, subunit IV MW 16000, SDS-PAGE, structure-function relationship of subunits
additional information
-
PetG is an essential subunit of the cytochrome b6f complex
additional information
PetG is an essential subunit of the cytochrome b6f complex
additional information
PetG is an essential subunit of the cytochrome b6f complex
additional information
-
PetL is not an essential subunit of the cytochrome b6f complex
additional information
PetL is not an essential subunit of the cytochrome b6f complex
additional information
PetL is not an essential subunit of the cytochrome b6f complex
additional information
-
PetN is an essential subunit of the cytochrome b6f complex
additional information
PetN is an essential subunit of the cytochrome b6f complex
additional information
PetN is an essential subunit of the cytochrome b6f complex
additional information
-
complex consists of polypeptides with the following molecular weights: 35000, 23000, 20000, 16000, SDS-PAGE
additional information
-
complex consists of the following polypeptides: cytochrome f MW 31000, cytochrome b6 MW 22000, Rieske FeS protein MW 22000, and a polypeptide with the molecular weight of 16000, SDS-PAGE
additional information
-
ratio cytochrome b563:cytochrome f:Rieske Fe-S protein 2:1:1
additional information
-
ratio cytochrome b563:cytochrome f:Rieske Fe-S protein 2:1:1
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method using 1.5 M [NH4]2SO4, 100 mM sodium acetate at pH 4.6
-
modeling of the first step of plastoquinol PQH2 oxidation by the iron-sulfur protein of the Cyt b6f complex. The H-transfer reaction displays a bidirectional mechanism, an electron is directed to the Fe(1) atom of the [Fe2S2] cluster of the iron-sulfur protein, and a proton is accepted by the Nepsilon atom of the His155 residue liganding the Fe(1) atom. Results support a diabatic model of the H-transfer, which implies that the elementary steps of electron and proton transfer occur much more rapidly than the concomitant changes in the system geometry
3.0 A crystal structure, native enzyme and enzyme in complex with 8-hydroxy-5,7-dimethoxy-3-methyl-2-tridecyl-4H-chromen-4-one or with 2,5-dibromo-5-methyl-6-isopropyl-benzoquinone
-
free enzyme and enzyme complexed with with quinone analogue inhibitors tridecyl-stigmatellin and 2-nonyl-4-hydroxyquinoline N-oxide, X-ray diffraction structure determination at 2.70 A, 3.07 A, and 3.25 A resolution, respectively
-
hanging drop vapour diffuion method, 0.0015 ml protein solution, containing 0.135-0.18 mM protein, is mixed with 0.0015 ml of reservoir solution, containing 100 mM Tris-HCl, pH 8.5, 200 mM MgCl2, 40 mM CdCl2, and 16?17% PEG-550 monomethyl ether, 4 °C, hexagonal bipyramidal crystals appear in 24?36 h, X-ray diffraction structure determination at 2.8 A resolution
hanging-drop vapor diffusion. A native structure of the cytochrome b6f complex with improved resolution is obtained from crystals of the complex grown in the presence of divalent cadmium
modeling of the first step of plastoquinol PQH2 oxidation by the iron-sulfur protein of the Cyt b6f complex. The H-transfer reaction displays a bidirectional mechanism, an electron is directed to the Fe(1) atom of the [Fe2S2] cluster of the iron-sulfur protein, and a proton is accepted by the Nepsilon atom of the His155 residue liganding the Fe(1) atom. Results support a diabatic model of the H-transfer, which implies that the elementary steps of electron and proton transfer occur much more rapidly than the concomitant changes in the system geometry
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
P194L
-
mutation in the Rieske subunit of the cytochrome b6/f complex is characterized by a reduced electron transport activity at saturating light intensities in vivo. The electron transfer from cytochrome b6/f to photosystem I is not generally reduced in the mutant, but the pH dependence of the reaction is altered
S154A
-
results in a 97 mV decrease in the midpoint potential relative to the wild-type and a 5fold decrease in sensitivity to inhibition by stigmatellin
S154C
-
results in a 17 mV increase in the midpoint potential relative to the wild-type
S154T
-
results in a 72 mV increase in the midpoint potential relative to the wild-type
Y156F
-
results in a 45 mV decrease in the midpoint potential relative to the wild-type
Y156W
-
results in a decrease in the midpoint potential by 100 mV and substantial changes in the EPR spectra relative to the wild-type enzyme
E78D
-
mutation in subunit IV, retained functional features of wild type configuration
E78K
E78L
-
mutation in subunit IV, decrease in the rate of the concerted oxidation process at the Q0 site
E78N
-
mutation in subunit IV, modified characteristics of cytochrome b6/f turnover under repetitive flash illumination
E78Q
F40Y
-
subunit IV mutation, in van der Waal's contact with the plane of ci heme
P2V
-
different stigmatellin-sensitive reduction kinetics compared to wild-type enzyme
P2V/R156A
-
different stigmatellin-sensitive reduction kinetics compared to wild-type enzyme
R156A
-
different stigmatellin-sensitive reduction kinetics compared to wild-type enzyme
A154G
-
increased resistance to 2,5-dibromo-3-methyl-6-isopropylbenzoquinone and stigmatellin
S159A
-
increased resistance to 2,5-dibromo-3-methyl-6-isopropylbenzoquinone
additional information
-
deletion of small domain of cytochrome f leads to changed kinetic parameters and faster degradation compared to the wild type enzyme
E78K
-
mutation in subunit IV, decrease in the rate of the concerted oxidation process at the Q0 site
E78K
-
comparison with wild-type values reveals that the mutated amino acid residue plays an essential role in plastoquinol oxidation at low pH, while it is not required for efficient activity at neutral pH, the residue is involved in gating the redox-coupled proton pumping activity
E78Q
-
mutation in subunit IV, modified characteristics of cytochrome b6/f turnover under repetitive flash illumination
E78Q
-
comparison with wild-type values reveals that the mutated amino acid residue plays an essential role in plastoquinol oxidation at low pH, while it is not required for efficient activity at neutral pH, the residue is involved in gating the redox-coupled proton pumping activity
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C
-70°C, 30 mM Tris-succinate buffer, pH 6.5, 1% sodium cholate, 10% glycerol
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation and hydroxyapatite column chromatography
-
nickel-affinity resin chromatography and hydrophobic interaction chromatography
-
partial purification from thylakoid membranes by ammonium sulfate precipitation and hydrophobic interaction chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
enzyme reacts with purified photosystem I reaction centers in the micellar state if plastocyanin is present
-
reconstitution into lipid vesicles
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gu, L.Q.; Yu, L.; Yu, C.A.
A ubiquinone derivative that inhibits mitochondrial cytochrome b-c1 complex but not chloroplast cytochrome b6-f complex activity
J. Biol. Chem.
264
4506-4512
1989
Spinacia oleracea
brenda
Malkin, R.
Cytochrome b/f6 complex in cyanobacteria: common components of respiratory and photosynthetic electron transport systems
Methods Enzymol.
167
341-349
1988
Trichormus variabilis
-
brenda
Stirewalt, V.L.; Bryant, D.A.
Molecular cloning and nucleotide sequence of the petG gene of the cyanelle genome of Cyanophora paradoxa
Nucleic Acids Res.
17
10095
1989
Cyanophora paradoxa
brenda
Adam, Z.; Malkin, R.
Reconstitution of isolated Rieske Fe-S protein into a Rieske-depleted cytochrome b6-f complex
FEBS Lett.
225
67-71
1987
Spinacia oleracea
brenda
Black, M.T.; Widger, W.R.; Cramer, W.A.
Large-scale purification of active cytochrome b6/f complex from spinach chloroplasts
Arch. Biochem. Biophys.
252
655-661
1987
Spinacia oleracea
brenda
Malkin, R.
Interaction of stigmatellin and DNP-INT with the Rieske iron-sulfur center of the chloroplast cytochrome b6-f complex
FEBS Lett.
208
317-320
1986
Spinacia oleracea
brenda
Lam, E.
Nearest-neighbor relationships of the constituent polypeptides in plastoquinol-plastocyanin oxidoreductase
Biochim. Biophys. Acta
848
324-332
1986
Spinacia oleracea
brenda
Phillis, A.L.; Gray, J.C.
Isolation and characterization of a cytochrome b-f complex from pea chloroplasts
Eur. J. Biochem.
137
553-560
1983
Pisum sativum
brenda
Hurt, E.C.; Gabellini, N.; Shahak, Y.; Lochau, W.; Hauska, G.
Extra proton translocation and membrane potential generation--universal properties of cytochrome bc1/b6f complexes reconstituted into liposomes
Arch. Biochem. Biophys.
225
879-885
1983
Trichormus variabilis, Spinacia oleracea
brenda
Clark, R.D.; Hind, G.
Isolation of a five-polypeptide cytochrome b-f complex from spinach chloroplasts
J. Biol. Chem.
258
10348-10354
1983
Spinacia oleracea
brenda
Oettmeier, W.; Masson, K.; Olschewski, E.
Photoaffinity labelling of chloroplast cytochrome b6-f complex by an inhibitor azido-derivate
FEBS Lett.
155
241-244
1983
Spinacia oleracea
-
brenda
Hauska, G.; Hurt, E.; Gabellini, N.; Lockau, W.
Comparative aspects of quinol-cytochrome c/plastocyanin oxidoreductases
Biochim. Biophys. Acta
726
97-133
1983
Spinacia oleracea, Trichormus variabilis
brenda
Hurt, E.; Hauska, G.; Malkin, R.
Isolation of the Rieske iron-sulfur protein from the cytochrome b6/f complex of spinach chloroplasts
FEBS Lett.
134
1-5
1981
Spinacia oleracea
brenda
Hurt, E.; Hauska, G.
A cytochrome f/b6 complex of five polypeptides with plastoquinol-plastocyanin-oxidoreductase activity from spinach chloroplasts
Eur. J. Biochem.
117
591-599
1981
Spinacia oleracea
brenda
Oettmeier, W.; Dostatni, R.; Majewski, C.; Hfle, G.; Fecker, T.; Kunze, B.; Reichenbach, H.
The aurachins, naturally occurring inhibitors of photosynthetic electron flow through photosystem II and the cytochrome b6/f-complex
Z. Naturforsch. C
45
322-328
1990
Spinacia oleracea
-
brenda
Kallas, T.; Malkin, R.
Isolation and characterization of genes for cytochrome b6/f complex
Methods Enzymol.
167
779-794
1988
Nostoc sp.
brenda
Doyle, M.P.; Li, L.B.; Yu, L.; Yu, C.A.
Identification of a Mr = 17,000 protein as the plastoquinone-binding protein in the cytochrome b6-f complex from spinach chloroplasts
J. Biol. Chem.
264
1387-1392
1989
Spinacia oleracea
brenda
Wynn, R.M.; Bertsch, J.; Bruce, B.D.; Malkin, R.
Green algal cytochrome b6-f complexes: isolation and characterization from Dunaliella saline, Chlamydomonas reinhardtii and Scenedesmus obliquus
Biochim. Biophys. Acta
935
115-122
1988
Chlamydomonas reinhardtii, Dunaliella salina, Tetradesmus obliquus
brenda
Hauska, G.
Preparation of electrogenic, proton-transporting cytochrome complexes of the b6f-type (chloroplasts and cyanobacteria) and bc1-type (Rhodopseudomonas sphaeroides)
Methods Enzymol.
126
271-285
1986
Trichormus variabilis, Spinacia oleracea
-
brenda
Morrissey, P.J.; McCauley, S.W.; Melis, A.
Differential detergent-solubilization of integral thylakoid membrane complexes in spinach chloroplasts. Localization of photosystem II, cytochrome b6-f complex and photosystem I
Eur. J. Biochem.
160
389-393
1986
Spinacia oleracea
brenda
Lemaire, C.; Girard-Bascou, J.; Wollman, F.A.; Bennoun, P.
Studies on the cytochrome b6/f complex. I. Characterization of the complex subunits in Chlamydomonas reinhardtii
Biochim. Biophys. Acta
851
229-238
1986
Chlamydomonas reinhardtii, Spinacia oleracea
-
brenda
Olive, J.; Vallon, O.; Wollman, F.A.; Recouvreur, M.; Bennoun, P.
Studies on the cytochrome b6/f complex. II. Localization of the complex in the thylakoid membranes from spinach and Chlamydomonas reinhardtii by immunocytochemistry and freeze fracture analysis of b6/f mutants
Biochim. Biophys. Acta
851
239-248
1986
Chlamydomonas reinhardtii
-
brenda
Melis, A.; Svensson, P.; Albertsson, P.A.
The domain organization of the chloroplast thylakoid membrane. Localization of photosystem I and the cytochrome b6/-f complex
Biochim. Biophys. Acta
850
402-412
1986
Spinacia oleracea
-
brenda
Allred, D.R.; Staehelin, L.A.
Spatial organization of the cytochrome b6-f complex within chloroplast thylakoid membranes
Biochim. Biophys. Acta
849
94-103
1986
Pisum sativum, Spinacia oleracea
brenda
Doyle, M.F.; Yu, C.A.
Preparation and reconstitution of a phospholipid deficient cytochrome b6-f complex from spinach chloroplasts
Biochem. Biophys. Res. Commun.
131
700-706
1985
Spinacia oleracea
brenda
Ortiz, W.; Malkin, R.
Topographical studies of the polypeptide subunits of the thylakoid cytochrome b6-f complex
Biochim. Biophys. Acta
808
164-170
1985
Spinacia oleracea
brenda
Krinner, M.; Hauska, G.; Hurt, E.; Lockau, W.
A cytochrome f-b6 complex with plastoquinol-cytochrome c oxidoreductase activity from Anabaena variabilis
Biochim. Biophys. Acta
681
110-117
1982
Trichormus variabilis
-
brenda
Hurt, E.C.; Hauska, G.; Shahak, Y.
Electrogenic proton translocation by the chloroplast cytochrome b6/f complex reconstituted into phospholipid vesicles
FEBS Lett.
149
211-216
1982
Spinacia oleracea
-
brenda
Rich, P.; Heathcote, P.; Moss, D.A.
Kinetic studies of electron transfer in a hybrid system constructed from the cytochrome bf complex and photosystem I
Biochim. Biophys. Acta
892
138-151
1987
Lactuca sp.
-
brenda
Breyton, C.; Tribet, C.; Olive, J.; Dubacq, J.P.; Popot, J.L.
Dimer to monomer conversion of the cytochrome b6 f complex. Causes and consequences
J. Biol. Chem.
272
21892-21900
1997
Chlamydomonas reinhardtii
brenda
Fernandez-Velasco, J.G.; Jamshidi, A.; Gong, X.S.; Zhou, J.; Ueng, R.Y.
Photosynthetic electron transfer through the cytochrome b6f complex can bypass cytochrome f
J. Biol. Chem.
276
30598-30607
2001
Chlamydomonas reinhardtii
brenda
Gong, X.S.; Chung, S.; Fernandez-Velasco, J.G.
Electron transfer and stability of the cytochrome b6f complex in a small domain deletion mutant of cytochrome f
J. Biol. Chem.
276
24365-24371
2001
Chlamydomonas reinhardtii
brenda
Lee, T.X.; Metzger, S.U.; Cho, Y.S.; Whitmarsh, J.; Kallas, T.
Modification of inhibitor binding sites in the cytochrome bf complex by directed mutagenesis of cytochrome b6 in Synechococcus sp. PCC 7002
Biochim. Biophys. Acta
1504
235-247
2001
Synechococcus sp.
brenda
Molik, S.; Karnauchov, I.; Weidlich, C.; Herrmann, R.G.; Klosgen, R.B.
The Rieske Fe/S protein of the cytochrome b6/f complex in chloroplasts: missing link in the evolution of protein transport pathways in chloroplasts?
J. Biol. Chem.
276
42761-42766
2001
Spinacia oleracea
brenda
Pierre, Y.; Breyton, C.; Kramer, D.; Popot, J.L.
Purification and characterization of the cytochrome b6 f complex from Chlamydomonas reinhardtii
J. Biol. Chem.
270
29342-29349
1995
Chlamydomonas reinhardtii
brenda
Roberts, A.G.; Bowman, M.K.; Kramer, D.M.
Certain metal ions are inhibitors of cytochrome b6f complex 'Rieske' iron-sulfur protein domain movements
Biochemistry
41
4070-4079
2002
Spinacia oleracea
brenda
Soriano, G.M.; Cramer, W.A.
Deuterium kinetic isotope effects in the p-side pathway for quinol oxidation by the cytochrome b6 f complex
Biochemistry
40
15109-15116
2001
Spinacia oleracea
brenda
Zito, F.; Finazzi, G.; Joliot, P.; Wollman, F.A.
Glu78, from the conserved PEWY sequence of subunit IV, has a key function in cytochrome b6f turnover
Biochemistry
37
10395-10403
1998
Chlamydomonas reinhardtii
brenda
Finazzi, G.
Redox-coupled proton pumping activity in cytochrome b6f, as evidenced by the pH dependence of electron transfer in whole cells of Chlamydomonas reinhardtii
Biochemistry
41
7475-7482
2002
Chlamydomonas reinhardtii
brenda
Roberts, A.G.; Bowman, M.K.; Kramer, D.M.
The ihibitor DBMIB povides isight into the functional architecture of the Qo site in the cytochrome b6f complex
Biochemistry
43
7707-7716
2004
Chlamydomonas reinhardtii, Mastigocladus laminosus
brenda
Jahns, P.; Graf, M.; Munekage, Y.; Shikanai, T.
Single point mutation in the Rieske iron-sulfur subunit of cytochrome b6/f leads to an altered pH dependence of plastoquinol oxidation in Arabidopsis
FEBS Lett.
519
99-102
2002
Arabidopsis thaliana
brenda
Schneider, D.; Berry, S.; Volkmer, T.; Seidler, A.; Roegner, M.
PetC1 is the major Rieske iron-sulfur protein in the cytochrome b6f complex of Synechocystis sp. PCC 6803
J. Biol. Chem.
279
39383-39388
2004
Synechocystis sp. PCC 6803
brenda
Whitelegge, J.P.; Zhang, H.; Aguilera, R.; Taylor, R.M.; Cramer, W.A.
Full subunit coverage liquid chromatography electrospray ionization mass spectrometry (LCMS+) of an oligomeric membrane protein: cytochrome b6f complex from spinach and the cyanobacterium Mastigocladus laminosus
Mol. Cell. Proteomics
1
816-827
2002
Spinacia oleracea, Mastigocladus laminosus
brenda
Stroebel, D.; Choquet, Y.; Popot, J.L.; Picot, D.
An atypical haem in the cytochrome b6f complex
Nature
426
413-418
2003
Chlamydomonas reinhardtii
brenda
Kurisu, G.; Zhang, H.; Smith, J.L.; Cramer, W.A.
Structure of the cytochrome b6f complex of oxygenic photosynthesis: tuning the cavity
Science
302
1009-1014
2003
Mastigocladus laminosus
brenda
Popescu, C.E.; Borza, T.; Bielawski, J.P.; Lee, R.W.
Evolutionary rates and expression level in Chlamydomonas
Genetics
172
1567-1576
2006
Chlamydomonas incerta, Chlamydomonas incerta SAG 7.73
brenda
Zatsman, A.I.; Zhang, H.; Gunderson, W.A.; Cramer, W.A.; Hendrich, M.P.
Heme-heme interactions in the cytochrome b6f complex: EPR spectroscopy and correlation with structure
J. Am. Chem. Soc.
128
14246-14247
2006
Cyanobacterium sp.
brenda
Finazzi, G.
The central role of the green alga Chlamydomonas reinhardtii in revealing the mechanism of state transitions
J. Exp. Bot.
56
383-388
2005
Chlamydomonas reinhardtii, Mastigocladus laminosus
brenda
Nosenko, T.; Lidie, K.L.; Van Dolah, F.M.; Lindquist, E.; Cheng, J.; Bhattacharya, D.
Chimeric plastid proteome in the florida "red tide" dinoflagellate Karenia brevis
Mol. Biol. Evol.
23
2026-2038
2006
Karenia brevis (Q00GM2)
brenda
Endo, T.; Kawase, D.; Sato, F.
Stromal over-reduction by high-light stress as measured by decreases in P700 oxidation by far-red light and its physiological relevance
Plant Cell Physiol.
46
775-781
2005
Commelina communis, Desmodium paniculatum, Quercus glauca
brenda
Rosso, D.; Ivanov, A.G.; Fu, A.; Geisler-Lee, J.; Hendrickson, L.; Geisler, M.; Stewart, G.; Krol, M.; Hurry, V.; Rodermel, S.R.; Maxwell, D.P.; Huner, N.P.
IMMUTANS does not act as a stress-induced safety valve in the protection of the photosynthetic apparatus of Arabidopsis during steady-state photosynthesis
Plant Physiol.
142
574-585
2006
Arabidopsis thaliana
brenda
Alric, J.; Pierre, Y.; Picot, D.; Lavergne, J.; Rappaport, F.
Spectral and redox characterization of the heme ci of the cytochrome b6f complex
Proc. Natl. Acad. Sci. USA
102
15860-15865
2005
Chlamydomonas reinhardtii
brenda
Kolling, D.J.; Brunzelle, J.S.; Lhee, S.; Crofts, A.R.; Nair, S.K.
Atomic resolution structures of Rieske iron-sulfur protein: role of hydrogen bonds in tuning the redox potential of iron-sulfur clusters
Structure
15
29-38
2007
Cereibacter sphaeroides
brenda
Reisinger, V.; Hertle, A.P.; Ploescher, M.; Eichacker, L.A.
Cytochrome b6f is a dimeric protochlorophyll a binding complex in etioplasts
FEBS J.
275
1018-1024
2008
Hordeum vulgare
brenda
Schoettler, M.A.; Fluegel, C.; Thiele, W.; Bock, R.
Knock-out of the plastid-encoded PetL subunit results in reduced stability and accelerated leaf age-dependent loss of the cytochrome b6f complex
J. Biol. Chem.
282
976-985
2007
Nicotiana tabacum
brenda
Lezhneva, L.; Kuras, R.; Ephritikhine, G.; de Vitry, C.
A novel pathway of cytochrome c biogenesis is involved in the assembly of the cytochrome b6f complex in Arabidopsis chloroplasts
J. Biol. Chem.
283
24608-24616
2008
Arabidopsis sp.
brenda
Yamashita, E.; Zhang, H.; Cramer, W.A.
Structure of the cytochrome b6f complex: quinone analogue inhibitors as ligands of heme cn
J. Mol. Biol.
370
39-52
2007
Mastigocladus laminosus (P83791)
brenda
Dashdorj, N.; Yamashita, E.; Schaibley, J.; Cramer, W.A.; Savikhin, S.
Ultrafast optical pump-probe studies of the cytochrome b(6)f complex in solution and crystalline states
J. Phys. Chem. B
111
14405-14410
2007
Mastigocladus laminosus
brenda
Lyska, D.; Paradies, S.; Meierhoff, K.; Westhoff, P.
HCF208, a homolog of Chlamydomonas CCB2, is required for accumulation of native cytochrome b6 in Arabidopsis thaliana
Plant Cell Physiol.
48
1737-1746
2007
Arabidopsis thaliana
brenda
Schwenkert, S.; Legen, J.; Takami, T.; Shikanai, T.; Herrmann, R.G.; Meurer, J.
Role of the low-molecular-weight subunits PetL, PetG, and PetN in assembly, stability, and dimerization of the cytochrome b6f complex in tobacco
Plant Physiol.
144
1924-1935
2007
Nicotiana tabacum
brenda
Schneider, D.; Volkmer, T.; Roegner, M.
PetG and PetN, but not PetL, are essential subunits of the cytochrome b6f complex from Synechocystis PCC 6803
Res. Microbiol.
158
45-50
2007
Synechocystis sp., Synechocystis sp. (P72717), Synechocystis sp. (P74149)
brenda
Yan, J.; Dashdorj, N.; Baniulis, D.; Yamashita, E.; Savikhin, S.; Cramer, W.A.
On the structural role of the aromatic residue environment of the chlorophyll a in the cytochrome b6f complex
Biochemistry
47
3654-3661
2008
Synechococcus sp. PCC 7002
brenda
de Lacroix de Lavalette, A.; Barucq, L.; Alric, J.; Rappaport, F.; Zito, F.
Is the redox state of the ci heme of the cytochrome b6f complex dependent on the occupation and structure of the Qi site and vice versa?
J. Biol. Chem.
284
20822-20829
2009
Chlamydomonas reinhardtii
brenda
Baniulis, D.; Yamashita, E.; Whitelegge, J.P.; Zatsman, A.I.; Hendrich, M.P.; Hasan, S.S.; Ryan, C.M.; Cramer, W.A.
Structure-Function, Stability, and Chemical Modification of the Cyanobacterial Cytochrome b6f Complex from Nostoc sp. PCC 7120
J. Biol. Chem.
284
9861-9869
2009
Nostoc sp. PCC 7120 = FACHB-418
brenda
Baniulis, D.; Yamashita, E.; Zhang, H.; Hasan, S.S.; Cramer, W.A.
Structure-function of the cytochrome b6f complex
Photochem. Photobiol.
84
1349-1358
2008
Chlamydomonas reinhardtii, Mastigocladus laminosus
brenda
Sang, M.; Ma, F.; Xie, J.; Chen, X.B.; Wang, K.B.; Qin, X.C.; Wang, W.D.; Zhao, J.Q.; Li, L.B.; Zhang, J.P.; Kuang, T.Y.
High-light induced singlet oxygen formation in cytochrome b6f complex from Bryopsis corticulans as detected by EPR spectroscopy
Biophys. Chem.
146
7-12
2010
Bryopsis corticulans
brenda
Twigg, A.I.; Baniulis, D.; Cramer, W.A.; Hendrich, M.P.
EPR detection of an O2 surrogate bound to heme cn of the cytochrome b6f complex
J. Am. Chem. Soc.
131
12536-12537
2009
Spinacia oleracea
brenda
Romanowska, E.
Isolation of cytochrome b6f complex from grana and stroma membranes from spinach chloroplasts
Methods Mol. Biol.
684
53-64
2011
Spinacia oleracea
brenda
Baniulis, D.; Zhang, H.; Zakharova, T.; Hasan, S.S.; Cramer, W.A.
Purification and crystallization of the cyanobacterial cytochrome b6f complex
Methods Mol. Biol.
684
65-77
2011
Nostoc sp., Spinacia oleracea, Mastigocladus laminosus, Nostoc sp. PCC 7120
brenda
Ma, F.; Chen, X.B.; Sang, M.; Wang, P.; Zhang, J.P.; Li, L.B.; Kuang, T.Y.
Singlet oxygen formation and chlorophyll a triplet excited state deactivation in the cytochrome b6f complex from Bryopsis corticulans
Photosynth. Res.
100
19-28
2009
Bryopsis corticulans
brenda
Hasan, S.S.; Stofleth, J.T.; Yamashita, E.; Cramer, W.A.
Lipid-induced conformational changes within the cytochrome b6f complex of oxygenic photosynthesis
Biochemistry
52
2649-2654
2013
Mastigocladus laminosus (P83791)
brenda
Mulkidjanian, A.
Activated Q-cycle as a common mechanism for cytochrome bc1 and cytochrome b6f complexes
Biochim. Biophys. Acta
1797
1858-1868
2010
Rhodobacter capsulatus
brenda
Hasan, S.S.; Yamashita, E.; Baniulis, D.; Cramer, W.A.
Quinone-dependent proton transfer pathways in the photosynthetic cytochrome b6f complex
Proc. Natl. Acad. Sci. USA
110
4297-4302
2013
Mastigocladus laminosus
brenda
Singh, S.K.; Hasan, S.S.; Zakharov, S.D.; Naurin, S.; Cohn, W.; Ma, J.; Whitelegge, J.P.; Cramer, W.A.
Trans-membrane signaling in photosynthetic state transitions redox- and structure-dependent interaction in vitro between STT7 kinase and the cytochrome b6f complex
J. Biol. Chem.
291
21740-21750
2016
Nostoc sp. PCC 7120 = FACHB-418 (Q93SX0)
brenda
Shapiguzov, A.; Chai, X.; Fucile, G.; Longoni, P.; Zhang, L.; Rochaix, J.D.
Activation of the Stt7/STN7 kinase through dynamic interactions with the cytochrome b6f complex
Plant Physiol.
171
82-92
2016
Chlamydomonas reinhardtii
brenda
Ustynyuk, L.; Tikhonov, A.
The cytochrome b6f complex DFT modeling of the first step of plastoquinol oxidation by the iron-sulfur protein
J. Organomet. Chem.
867
290-299
2018
Chlamydomonas reinhardtii (P23577), Mastigocladus laminosus (P83791)
-
brenda
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