Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.97.1.12 - photosystem I and Organism(s) Chlamydomonas reinhardtii and UniProt Accession P09144

for references in articles please use BRENDA:EC1.97.1.12
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Chlamydomonas reinhardtii
UNIPROT: P09144
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Chlamydomonas reinhardtii
The enzyme appears in selected viruses and cellular organisms
Synonyms
photosystem i, psi core complex, ps-i complex, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
photosystem I P700 chlorophyll a apoprotein A2
-
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
?
-
photo-oxidation of P700 causes a broad increase in absorption in the near-infrared region due to presence of a chlorophyll cation radical (P700+)
-
-
?
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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
beta-carotene
-
-
chlorophyll a
-
most abundant cofactor in PSI, role of these molecules in light absorption, charge separation, electron transfer, and biogenesis
chlorophyll a'
-
one member of the P700 special pair is a chlorophyll a' molecule
iron-sulfur centre
-
a PSI complex contains 12 iron atoms that constitute 3 [4Fe-4S] clusters
Lipid
-
four lipid molecules can be assigned in the high-resolution structure of PSI. Three of these molecules are phosphatidylglycerol and one is monogalactosyldiacylglycerol. These molecules are embedded in the PSI complex, with the acyl chains anchored among transmembrane helices. The phosphodiester group of one of the phospholipids coordinates an antenna chlorophyll molecule
phylloquinone
additional information
the electron-transfer cofactors are arranged in two nearly symmetric branches extending across the membrane from P700, which is a dimer of Chl a and a C-13 epimer of Chl a. Each branch contains an additional pair of Chl a molecules (ec2A/ec3A or ec2B/ec3B) and a phylloquinone (PhQA or PhQB), overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
kinetics of electron transfer of wild-type and mutant enzymes, overview
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
assay at room temperature
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
subunit PsaB
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
additional information
in photosystem I, light-induced electron transfer can occur in either of two symmetry-related branches of cofactors, each of which is composed of a pair of chlorophylls (ec2A/ec3A or ec2B/ec3B) and a phylloquinone (PhQA or PhQB). The axial ligand to the central Mg2+ of the ec2A and ec2B chlorophylls is a water molecule that is also H-bonded to a nearby Asn residue, an important interaction for charge separation by converting each of the Asn residues to a Leu in the green alga, Chlamydomonas reinhardtii. Each branch of the reaction center appears to operate independently of the other in carrying out light-induced charge separation
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PSAB_CHLRE
735
9
82109
Swiss-Prot
Mitochondrion (Reliability: 4)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trimer
cyanobacterial PSI is usually trimeric
additional information
-
plant and algal PSI complexes contain 14-15 protein subunits. Of these, only PsaA, PsaB, and PsaC bind the cofactors of the electron transfer system. PsaA and PsaB form the core complex around which other subunits are organized. The PsaC, PsaD, PsaH, and PsaE proteins form the stromal peripheral domain that contains the terminal electron donors and the ferredoxin-docking site. PsaN of plant and algal PSI is a lumenal peripheral protein. PsaN and the large lumenal domain of PsaF form the plastocyanin docking site of plant and algal PSI. The remaining proteins of PSI are integral membrane proteins with 1–3 transmembrane helices. The function of the PSI proteins
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
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
F689N
site-directed mutagenesis of subunit PsaA, the mutation causes in an about 100fold decrease in the observed rate of cofactor phylloquinone PhQA- oxidation, resulting in a lifetime that exceeds that of the terminal electron donor, P700+. This situation allows a second photochemical charge separation event to be initiated before PhQA- has decayed, thereby mimicking in PSI a situation that occurs in type II reaction centers. Simulation of the pump-pump kinetics in PsaA-F689N, overview
N591L
site-directed mutagenesis of psaB, the mutant shows structural differences and altered activity compared to the wild-type enzyme, detailed overview
N604L
site-directed mutagenesis of psaA, the mutant shows structural differences and altered activity compared to the wild-type enzyme, detailed overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
rapid, high-yield purification of PS1
-
recombinant His6-tagged enzyme from thylakoid membranes by nickel affinity chromatography and ultrafiltration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chitnis, P.R.
Photosystem I: function and physiology
Annu. Rev. Plant Physiol. Plant Mol. Biol.
52
593-626
2001
Synechocystis sp., Arabidopsis thaliana, Chlamydomonas reinhardtii
Manually annotated by BRENDA team
Gulis, G.; Narasimhulu, K.V.; Fox, L.N.; Redding, K.E.
Purification of His6-tagged photosystem I from Chlamydomonas reinhardtii
Photosynth. Res.
96
51-60
2008
Chlamydomonas reinhardtii
Manually annotated by BRENDA team
Kuhlgert, S.; Drepper, F.; Fufezan, C.; Sommer, F.; Hippler, M.
Residues PsaB Asp612 and PsaB Glu613 of photosystem I confer pH-dependent binding of plastocyanin and cytochrome c 6
Biochemistry
51
7297-7303
2012
Chlamydomonas reinhardtii (P09144), Chlamydomonas reinhardtii
Manually annotated by BRENDA team
Badshah, S.; Sun, J.; Mula, S.; Gorka, M.; Baker, P.; Luthra, R.; Lin, S.; van der Est, A.; Golbeck, J.; Redding, K.
Mutations in algal and cyanobacterial photosystem I that independently affect the yield of initial charge separation in the two electron transfer cofactor branches
Biochim. Biophys. Acta
1859
42-55
2018
Chlamydomonas reinhardtii (P12154 AND P09144 AND Q00914), Synechocystis sp. PCC 6803 (P29254 AND P29255 AND P32422)
Manually annotated by BRENDA team
Santabarbara, S.; Bullock, B.; Rappaport, F.; Redding, K.
Controlling electron transfer between the two cofactor chains of photosystem I by the redox state of one of their components
Biophys. J.
108
1537-1547
2015
Chlamydomonas reinhardtii (P12154 AND P09144 AND Q00914), Chlamydomonas reinhardtii KRC91-1A (P12154 AND P09144 AND Q00914)
Manually annotated by BRENDA team