Information on EC 1.97.1.12 - photosystem I

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.97.1.12
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RECOMMENDED NAME
GeneOntology No.
photosystem I
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
reduced plastocyanin + oxidized ferredoxin + hnu = oxidized plastocyanin + reduced ferredoxin
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
photosynthesis
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photosynthesis light reactions
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SYSTEMATIC NAME
IUBMB Comments
plastocyanin:ferredoxin oxidoreductase (light-dependent)
Contains chlorophyll, phylloquinones, carotenoids and [4Fe-4S] clusters. Cytochrome c6 can act as an alternative electron donor, and flavodoxin as an alternative acceptor in some species.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
photosystem I reaction center subunit III, plastocyanin-docking protein
SwissProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
reduced plastocyanin + oxidized ferredoxin + hv
oxidized plastocyanin + reduced ferredoxin
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
reduced plastocyanin + oxidized ferredoxin + hv
oxidized plastocyanin + reduced ferredoxin
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
beta-carotene
Chlorophyll
chlorophyll a
chlorophyll a'
Ferredoxin
iron-sulfur centre
phylloquinone
[4Fe-4S] center
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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variations in the luminal Mg(II) concentration may modulate the binding between plastocyanin and photosystem I subunit PsaF during the light-dark transitions, being stronger in the illuminated state. The Mg(II) ion probably is bound close to Glu43 in the lower acidic patch, and most likely in the form of a hexaquo complex embedded within the hydration shell of plastocanin, suggesting a specific binding site for Mg(II) that may regulate the binding of plastocyanin to photosystem 1 in vivo
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ag(I)-substituted plastocyanin
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competitive inhibitor of the reaction with normal Cu-containg plastocyanin
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Zn(II)-substituted plastocyanin
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competitive inhibitor of the reaction with normal Cu-containg plastocyanin
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.007
reduced plastocyanin
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pH and temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03
Ag(I)-substituted plastocyanin
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pH and temperature not specified in the publication
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0.41
Zn(II)-substituted plastocyanin
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pH and temperature not specified in the publication
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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21000-22000 Da, photosystem 1 subunit PsaF that is involved in the docking of the electron-donor proteins plastocyanin and cytochrome c6, SDS-PAGE
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3.3 A crystal structure of the entire PSI super-complex, sitting drop variant of the vapor-diffusion technique at 4C
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sitting-drop variant of the vapour-diffusion technique at 4C, crystals diffract to 4 A resolution using synchrotron radiation and belong to the monoclinic crystal system, space group P21, with unit-cell parameters a = 181.90, b = 190.24, c = 219.66 A, beta = 90.484
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single crystals from a complex of photosystem I with ferredoxin are grown using PEG 400 and CaCl2 as precipitation agents. The crystals diffract X-rays to a resolution of 78 A. The space group iss determined to be orthorhombic with the unit cell dimensions a = 194 A, b = 208 A, and c = 354 A. The crystals contain photosystem I and ferredoxin in a 1:1 ratio. Electron paramagnetic resonance (EPR) measurements on these crystals are reported, where EPR signals of the three [4Fe-4S] clusters FA, FB, FX, and the [2Fe-2S] cluster of ferredoxin are detected
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highly ordered two-dimensional crystals of photosystem I reaction center complex
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isolation and reconstitution of the functional PSI complexes into 2D arrays. The solubilized and crystallized PSI has essentially the same protein composition, as shown by SDS/polyacrylamide gels
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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a group of short amphiphilic peptides improve the thermal stability of the multi-domain protein complex photosystem-I in aqueous solution. Ac-I5K2-CONH2 shows the best stabilizing effect by enhancing the melting temperature of PS-I from 48C to 53C at concentration of 0.65 mM and extending the half life of isolated PS-I significantly
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
a group of short amphiphilic peptides improve the thermal stability of the multi-domain protein complex photosystem-I in aqueous solution. Ac-I5K2-CONH2 shows the best stabilizing effect by enhancing the melting temperature of PS-I from 48C to 53C at concentration of 0.65 mM and extending the half life of isolated PS-I significantly
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acetyl-VVVVVVD stabilizes the photosystem I complex to a lesser extent than acetyl-AAAAAAK
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dodecyl-beta-D-maltoside partially stabilizes
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in the presence of acetyl-AAAAAAK, the PS-I complex is stable in a dried form at room temperature for at least 3 weeks
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octyl-beta-D-glucoside partially stabilizes
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
PsaE protein is purified to homogeneity by affinity chromatography. Subunit PsaE (a peripheral subunit of the PSI complex)is involved in the docking of ferredoxin/flavodoxin to the PSI complex and also participates in the cyclic electron transfer around phosposystem I
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purification of the luminal domain of spinach photosystem 1 subunit PsaF
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rapid, high-yield purification of PS1
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning of the luminal domain of spinach photosystem 1 subunit PsaF, expressed in Escherichia coli BL21 (DE3) using a pET32 Xa/LIC thioredoxin fusion system
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the psaE gene is cloned and overexpressed in Escherichia coli. PsaE (a peripheral subunit of the PSI complex) is involved in the docking of ferredoxin/flavodoxin to the PSI complex and also participates in the cyclic electron transfer around phosposystem I
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D612H/E613H
mutation in subunit PsaB of photosystem I. Photosystem I harboring the has a high affinity toward binding of the electron donors and possesses an altered pH dependence of electron transfer with plastocyanin and cytochrome c6. The mutant strain exhibits a strong light sensitive growth phenotype, indicating that decelerated turnover between plastocyanin/cytochrome c6 and photosystem I with respect to electron transfer is deleterious to the cells
F647C
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mutant strain cannot grow under photoautotrophic conditions because of low photosystem I activity, possibly due to low levels of proteins
F649C/G650I
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mutant strain cannot grow under photoautotrophic conditions because of low photosystem I activity, possibly due to low levels of proteins
H651C/L652M
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mutant strain cannot grow under photoautotrophic conditions because of low photosystem I activity, possibly due to low levels of proteins
S641C/V642I
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mutation in subunit PsaB. Mutant strain grows photoautotrophically and shows no obvious reduction in the photosystem I activity. Kinetics of P700 re-reduction by plastocyanin remains unaltered
W643C/A644I
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mutation in subunit PsaB. Mutant strain grows photoautotrophically and shows no obvious reduction in the photosystem I activity. Kinetics of P700 re-reduction by plastocyanin remains unaltered
W645C
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mutation in subunit PsaB. Mutant strain grows photoautotrophically and shows no obvious reduction in the photosystem I activity. Kinetics of P700 re-reduction by plastocyanin remains unaltered
additional information
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molecular analysis of spontaneous revertants from the mutants H651C/L652M, F649C/G650I and F647C suggests that an aromatic residue at F647 and a small residue at G650 may be necessary for maintaining the structural integrity of photosystem I
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