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Information on EC 1.97.1.12 - photosystem I and Organism(s) Thermosynechococcus vestitus and UniProt Accession P0A405

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IUBMB Comments
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.
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Thermosynechococcus vestitus
UNIPROT: P0A405 not found.
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Word Map
The enzyme appears in selected viruses and cellular organisms
Synonyms
photosystem i, psi core complex, ps-i complex, more
PATHWAY SOURCE
PATHWAYS
-
-, -
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.
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
additional information
?
-
Thermosynechococcus vestitus
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reduction of ferredoxin by photosystem I (PSI) involves the [4Fe-4S] clusters FA and FB harbored by subunit PsaC, with FB being the direct electron transfer partner of ferredoxin. Assay in presence of 5 mM MgCl2, 30 mM NaCl and 0.03% beta-dodecyl-maltoside, with 1-2.5 mM sodium ascorbate and 0.008-0.025 mM 2,6-dichlorophenolindophenol
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-
?
NATURAL SUBSTRATE
NATURAL 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
Thermosynechococcus vestitus
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-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
[4Fe-4S]-center
Thermosynechococcus vestitus
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reduction of ferredoxin by photosystem I (PSI) involves the [4Fe-4S] clusters FA and FB harbored by subunit PsaC, with FB being the direct electron transfer partner of ferredoxin
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
gallium ferredoxin
Thermosynechococcus vestitus
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binding of the redox-inactive gallium ferredoxin to PSI inhibits the electron transport reaction, binds to PSI competitively with ferredoxin suggesting a single ferredoxin?binding site in PSI, kinetics
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
Thermosynechococcus vestitus
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thermodynamics and kinetics
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
Thermosynechococcus vestitus
assay at
8
Thermosynechococcus vestitus
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Thermosynechococcus vestitus
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Thermosynechococcus vestitus
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PS I binding analysis using redox-inactive gallium ferredoxin, overview. Gallium ferredoxin binds to PSI competitively with ferredoxin suggesting a single ferredoxin?binding site in PSI, kinetics
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
Thermosynechococcus vestitus
inside the trimer, subunits PsaL, PsaI and PsaM (5 alpha-helices in total) are located in the center of the trimerization domain of PSI, thereby forming most of the contacts between the monomers
trimer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 100
Thermosynechococcus vestitus
analysis of thermostability of oligomeric PSI complexes. The thermal profile of the spectral shift of alpha-helices bands confirms the same two temperature intervals for PSI monomers and only one interval for trimers. Spectra at 20-100°C show distinct changes in the Amide I region of PSI complexes as a function of the rising temperature. Absorbance at the Amide I maximum of PSI monomers, gradually drops in two temperature intervals, i.e. 60-75°C and 80-90°C. In contrast, absorbance at the Amide I maximum of PSI trimers drops only in one temperature interval 80-95°C. Spectral changes of PSI trimers and monomers heated up to 100°C are irreversible due to protein denaturation and non-specific aggregation of complexes leading to new absorption bands. Thermal denaturation profiles, detailed overview, The enzyme shows denaturation at the monomer-monomer-interface at over 60°C, and denaturation/aggregation at the trimer-lipid interface at over 80°C. Oligomerization is one strategy to increase thermostability of PSI complexes
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mignee, C.; Mutoh, R.; Krieger-Liszkay, A.; Kurisu, G.; Setif, P.
Gallium ferredoxin as a tool to study the effects of ferredoxin binding to photosystem I without ferredoxin reduction
Photosynth. Res.
134
251-263
2017
Thermosynechococcus vestitus, Synechocystis sp. PCC 6803 (P29254 AND P29255 AND P32422)
Manually annotated by BRENDA team
Shubin, V.; Terekhova, I.; Bolychevtseva, Y.; El-Mohsnawy, E.; Roegner, M.; Maentele, W.; Kopczak, M.; Dzafic, E.
Thermostability of photosystem I trimers and monomers from the cyanobacterium Thermosynechococcus elongatus
Spectrochim. Acta A
179
17-22
2017
Thermosynechococcus vestitus (P0A405 AND P0A407 AND P0A415)
Manually annotated by BRENDA team