BRENDA - Enzyme Database show
show all sequences of 1.97.1.12

Mutations in algal and cyanobacterial photosystem I that independently affect the yield of initial charge separation in the two electron transfer cofactor branches

Badshah, S.; Sun, J.; Mula, S.; Gorka, M.; Baker, P.; Luthra, R.; Lin, S.; van der Est, A.; Golbeck, J.; Redding, K.; Biochim. Biophys. Acta 1859, 42-55 (2018)

Data extracted from this reference:

Engineering
Amino acid exchange
Commentary
Organism
N591L
site-directed mutagenesis of psaB, the mutant shows structural differences and altered activity compared to the wild-type enzyme, detailed overview
Chlamydomonas reinhardtii
N591L
site-directed mutagenesis of psaB, the mutant shows structural differences and altered activity compared to the wild-type enzyme, detailed overview
Synechocystis sp. PCC 6803
N604L
site-directed mutagenesis of psaA, the mutant shows structural differences and altered activity compared to the wild-type enzyme, detailed overview
Chlamydomonas reinhardtii
N604L
site-directed mutagenesis of psaA, the mutant shows structural differences and altered activity compared to the wild-type enzyme, detailed overview
Synechocystis sp. PCC 6803
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
thylakoid
-
Synechocystis sp. PCC 6803
9579
-
thylakoid
-
Chlamydomonas reinhardtii
9579
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
reduced plastocyanin + oxidized ferredoxin + hv
Synechocystis sp. PCC 6803
-
oxidized plastocyanin + reduced ferredoxin
-
-
?
reduced plastocyanin + oxidized ferredoxin + hv
Chlamydomonas reinhardtii
-
oxidized plastocyanin + reduced ferredoxin
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Chlamydomonas reinhardtii
P12154 AND P09144 AND Q00914
psaA, psaB, and psaC
-
Synechocystis sp. PCC 6803
P29254 AND P29255 AND P32422
psaA, psaB, and psaC
-
Purification (Commentary)
Commentary
Organism
recombinant His6-tagged enzyme from thylakoid membranes by nickel affinity chromatography and ultrafiltration
Chlamydomonas reinhardtii
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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+)
744412
Synechocystis sp. PCC 6803
?
-
-
-
-
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+)
744412
Chlamydomonas reinhardtii
?
-
-
-
-
reduced plastocyanin + oxidized ferredoxin + hv
-
744412
Synechocystis sp. PCC 6803
oxidized plastocyanin + reduced ferredoxin
-
-
-
?
reduced plastocyanin + oxidized ferredoxin + hv
-
744412
Chlamydomonas reinhardtii
oxidized plastocyanin + reduced ferredoxin
-
-
-
?
Subunits
Subunits
Commentary
Organism
trimer
cyanobacterial PSI is usually trimeric
Chlamydomonas reinhardtii
trimer
cyanobacterial PSI is usually trimeric
Synechocystis sp. PCC 6803
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
22
-
assay at room temperature
Chlamydomonas reinhardtii
22
-
assay at room temperature
Synechocystis sp. PCC 6803
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Chlamydomonas reinhardtii
7.5
-
assay at
Synechocystis sp. PCC 6803
Cofactor
Cofactor
Commentary
Organism
Structure
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
Chlamydomonas reinhardtii
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
Synechocystis sp. PCC 6803
phylloquinone
-
Chlamydomonas reinhardtii
phylloquinone
-
Synechocystis sp. PCC 6803
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
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
Chlamydomonas reinhardtii
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
Synechocystis sp. PCC 6803
phylloquinone
-
Chlamydomonas reinhardtii
phylloquinone
-
Synechocystis sp. PCC 6803
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
N591L
site-directed mutagenesis of psaB, the mutant shows structural differences and altered activity compared to the wild-type enzyme, detailed overview
Chlamydomonas reinhardtii
N591L
site-directed mutagenesis of psaB, the mutant shows structural differences and altered activity compared to the wild-type enzyme, detailed overview
Synechocystis sp. PCC 6803
N604L
site-directed mutagenesis of psaA, the mutant shows structural differences and altered activity compared to the wild-type enzyme, detailed overview
Chlamydomonas reinhardtii
N604L
site-directed mutagenesis of psaA, the mutant shows structural differences and altered activity compared to the wild-type enzyme, detailed overview
Synechocystis sp. PCC 6803
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
thylakoid
-
Synechocystis sp. PCC 6803
9579
-
thylakoid
-
Chlamydomonas reinhardtii
9579
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
reduced plastocyanin + oxidized ferredoxin + hv
Synechocystis sp. PCC 6803
-
oxidized plastocyanin + reduced ferredoxin
-
-
?
reduced plastocyanin + oxidized ferredoxin + hv
Chlamydomonas reinhardtii
-
oxidized plastocyanin + reduced ferredoxin
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His6-tagged enzyme from thylakoid membranes by nickel affinity chromatography and ultrafiltration
Chlamydomonas reinhardtii
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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+)
744412
Synechocystis sp. PCC 6803
?
-
-
-
-
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+)
744412
Chlamydomonas reinhardtii
?
-
-
-
-
reduced plastocyanin + oxidized ferredoxin + hv
-
744412
Synechocystis sp. PCC 6803
oxidized plastocyanin + reduced ferredoxin
-
-
-
?
reduced plastocyanin + oxidized ferredoxin + hv
-
744412
Chlamydomonas reinhardtii
oxidized plastocyanin + reduced ferredoxin
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
trimer
cyanobacterial PSI is usually trimeric
Chlamydomonas reinhardtii
trimer
cyanobacterial PSI is usually trimeric
Synechocystis sp. PCC 6803
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
22
-
assay at room temperature
Chlamydomonas reinhardtii
22
-
assay at room temperature
Synechocystis sp. PCC 6803
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Chlamydomonas reinhardtii
7.5
-
assay at
Synechocystis sp. PCC 6803
General Information
General Information
Commentary
Organism
malfunction
the PsaA-N604L mutation (near ec2B) results in a 50% reduction in the amount of electron transfer in the cofactor B-branch, while the PsaB-N591L mutation (near ec2A) results in a 70% reduction in the amount of electron transfer in the cofactor A-branch. The PsaB-N591L mutation had a significant effect upon trapping, while the PsaA-N604L mutation does not have a significant effect upon trapping
Chlamydomonas reinhardtii
malfunction
the PsaA-N604L mutation (near ec2B) results in a 50% reduction in the amount of electron transfer in the cofactor B-branch, while the PsaB-N591L mutation (near ec2A) results in a 70% reduction in the amount of electron transfer in the cofactor A-branch. The PsaB-N591L mutation had a significant effect upon trapping, while the PsaA-N604L mutation does not have a significant effect upon trapping
Synechocystis sp. PCC 6803
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
Chlamydomonas reinhardtii
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 cyanobacterium Synechocystis sp. PCC6803. Each branch of the reaction center appears to operate independently of the other in carrying out light-induced charge separation
Synechocystis sp. PCC 6803
physiological function
photosystem I (PSI) is a large pigment-protein complex that functions as a light-driven oxidoreductase, catalyzing an otherwise uphill electron transfer from cytochrome c or plastocyanin to ferredoxin or flavodoxin
Chlamydomonas reinhardtii
physiological function
photosystem I (PSI) is a large pigment-protein complex that functions as a light-driven oxidoreductase, catalyzing an otherwise uphill electron transfer from cytochrome c or plastocyanin to ferredoxin or flavodoxin
Synechocystis sp. PCC 6803
General Information (protein specific)
General Information
Commentary
Organism
malfunction
the PsaA-N604L mutation (near ec2B) results in a 50% reduction in the amount of electron transfer in the cofactor B-branch, while the PsaB-N591L mutation (near ec2A) results in a 70% reduction in the amount of electron transfer in the cofactor A-branch. The PsaB-N591L mutation had a significant effect upon trapping, while the PsaA-N604L mutation does not have a significant effect upon trapping
Chlamydomonas reinhardtii
malfunction
the PsaA-N604L mutation (near ec2B) results in a 50% reduction in the amount of electron transfer in the cofactor B-branch, while the PsaB-N591L mutation (near ec2A) results in a 70% reduction in the amount of electron transfer in the cofactor A-branch. The PsaB-N591L mutation had a significant effect upon trapping, while the PsaA-N604L mutation does not have a significant effect upon trapping
Synechocystis sp. PCC 6803
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
Chlamydomonas reinhardtii
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 cyanobacterium Synechocystis sp. PCC6803. Each branch of the reaction center appears to operate independently of the other in carrying out light-induced charge separation
Synechocystis sp. PCC 6803
physiological function
photosystem I (PSI) is a large pigment-protein complex that functions as a light-driven oxidoreductase, catalyzing an otherwise uphill electron transfer from cytochrome c or plastocyanin to ferredoxin or flavodoxin
Chlamydomonas reinhardtii
physiological function
photosystem I (PSI) is a large pigment-protein complex that functions as a light-driven oxidoreductase, catalyzing an otherwise uphill electron transfer from cytochrome c or plastocyanin to ferredoxin or flavodoxin
Synechocystis sp. PCC 6803
Other publictions for EC 1.97.1.12
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
744412
Badshah
Mutations in algal and cyanob ...
Chlamydomonas reinhardtii, Synechocystis sp. PCC 6803
Biochim. Biophys. Acta
1859
42-55
2018
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4
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4
2
2
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2
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6
6
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745118
Huang
-
Dual-located WHIRLY1 interact ...
Arabidopsis thaliana, Arabidopsis thaliana Col-0
Int. J. Mol. Sci.
18
E2352
2017
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1
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1
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2
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2
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24
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1
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2
1
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745870
Mazor
Structure of the plant photos ...
Pisum sativum
Nat. Plants
3
17014
2017
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1
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2
2
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745984
Huang
Superoxide generated in the c ...
Psychotria henryi
Photosyn. Res.
132
293-303
2017
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2
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3
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1
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8
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745985
Petrova
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Interaction of various types ...
Synechocystis sp. PCC 6803
Photosyn. Res.
133
175-184
2017
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1
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1
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5
1
1
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1
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2
2
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745986
Milanovsky
Kinetic modeling of electron ...
Synechocystis sp. PCC 6803
Photosyn. Res.
133
185-199
2017
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2
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745987
Mignee
Gallium ferredoxin as a tool ...
Synechocystis sp. PCC 6803, Thermosynechococcus elongatus
Photosyn. Res.
134
251-263
2017
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2
2
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6
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2
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2
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746500
Shubin
Thermostability of photosyste ...
Thermosynechococcus elongatus
Spectrochim. Acta A
179
17-22
2017
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744410
Strand
-
Redox regulation of the antim ...
Spinacia oleracea
Biochim. Biophys. Acta
1857
1-6
2016
2
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1
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744411
Semchonok
Cryo-EM structure of a tetram ...
Chroococcidiopsis sp. TS-821
Biochim. Biophys. Acta
1857
1619-1626
2016
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746044
Ishikawa
NDH-mediated cyclic electron ...
Flaveria bidentis
Plant Cell Physiol.
57
2020-2028
2016
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2
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744284
Kozuleva
-
The study of oxygen reduction ...
Pisum sativum
Biochemistry (Moscow)
9
246-251
2015
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Fromme
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Ruffle
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Ruffle
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Kinetic evidence for the PsaE- ...
Synechocystis sp.
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Lakshmi
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Biochemistry
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Surface analysis of the photos ...
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Almog
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