BRENDA - Enzyme Database show
show all sequences of 1.3.1.33

Mutagenesis alters the catalytic mechanism of the light-driven enzyme protochlorophyllide oxidoreductase

Menon, B.R.; Davison, P.A.; Hunter, C.N.; Scrutton, N.S.; Heyes, D.J.; J. Biol. Chem. 285, 2113-2119 (2009)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expressed in Escherichia coli; expression in Escherichia coli cells
Thermosynechococcus elongatus
Engineering
Amino acid exchange
Commentary
Organism
C199/C226S
mutant, mutation of the absolutely conserved cysteine residues
Thermosynechococcus elongatus
C199S
kcat comparable to wild-type, relative activity comparable to wild-type, Kd (NADPH) comparable to wild-type, Kd (protochlorophyllide) comparable to wild-type; mutant, Cys199 has a relatively minor role in catalysis
Thermosynechococcus elongatus
C199S/C226S
kcat more that 10fold decreased to wild-type, relative activity highly decreased compared to wild-type, Kd (NADPH) 2fold increased compared to wild-type, Kd (protochlorophyllide) 6fold increased compared to wild-type
Thermosynechococcus elongatus
C226S
kcat more that 10fold decreased to wild-type, relative activity highly decreased compared to wild-type, Kd (NADPH) comparable to wild-type, Kd (protochlorophyllide) 4fold increased compared to wild-type; mutant, mutation causes a remarkable change in the mechansim of the hydrogen transfer reactions
Thermosynechococcus elongatus
C37S
kcat comparable to wild-type, relative activity comparable to wild-type, Kd (NADPH) increased compared to wild-type, Kd (protochlorophyllide) equal to wild-type; mutant, Cys37 has a relatively minor role in catalysis
Thermosynechococcus elongatus
C37S/C199S
kcat comparable to wild-type, relative activity comparable to wild-type, Kd (NADPH) 10fold increased compared to wild-type, Kd (protochlorophyllide) comparable to wild-type; mutant, mutation of the absolutely conserved cysteine residues
Thermosynechococcus elongatus
C37S/C199S/C226S
kcat more that 10fold decreased to wild-type, relative activity highly decreased compared to wild-type, Kd (NADPH) 10fold increased compared to wild-type, Kd (protochlorophyllide) 6fold increased compared to wild-type; mutant, mutation of the absolutely conserved cysteine residues
Thermosynechococcus elongatus
C37S/C226S
kcat more that 10fold decreased to wild-type, relative activity highly decreased compared to wild-type, Kd (NADPH) 10fold increased compared to wild-type, Kd (protochlorophyllide) 6fold increased compared to wild-type; mutant, mutation of the absolutely conserved cysteine residues
Thermosynechococcus elongatus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
protochlorophyllide
mutant C199/C226S, relative activity 6.6%; mutant C199S, relative activity 98.2%; mutant C226S, relative activity 7.2%; mutant C37S/C199S/C226S, relative activity 7.1%; mutant C37S/C199S, relative activity 98.8%; mutant C37S/C226S, relative activity 6.8%; mutant C37S, relative activity 99.4%; wild type enzyme, relative activity 100%
Thermosynechococcus elongatus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
protochlorophyllide + NADPH
Thermosynechococcus elongatus
-
chlorophyllide + NADP+
-
-
?
protochlorophyllide + NADPH + H+
Thermosynechococcus elongatus
activation by light
chlorophyllide + NADP+
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Thermosynechococcus elongatus
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
protochlorophyllide + NADPH
-
699004
Thermosynechococcus elongatus
chlorophyllide + NADP+
-
-
-
?
protochlorophyllide + NADPH + H+
activation by light
699004
Thermosynechococcus elongatus
chlorophyllide + NADP+
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Thermosynechococcus elongatus
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.011
-
NADPH
pH 7.5, 25°C, mutant C199S/C226S, co-substrate: protochlorophyllide
Thermosynechococcus elongatus
0.011
-
protochlorophyllide
mutant C199/C226S; pH 7.5, 25°C, mutant C199S/C226S, co-substrate: NADPH
Thermosynechococcus elongatus
0.0113
-
NADPH
pH 7.5, 25°C, mutant C37S/C226S, co-substrate: protochlorophyllide
Thermosynechococcus elongatus
0.0113
-
protochlorophyllide
mutant C37S/C226S; pH 7.5, 25°C, mutant C37S/C226S, co-substrate: NADPH
Thermosynechococcus elongatus
0.0117
-
NADPH
pH 7.5, 25°C, mutant C37S/C199S/C226S, co-substrate: protochlorophyllide
Thermosynechococcus elongatus
0.0117
-
protochlorophyllide
mutant C37S/C199S/C226S; pH 7.5, 25°C, mutant C37S/C199S/C226S, co-substrate: NADPH
Thermosynechococcus elongatus
0.0118
-
NADPH
pH 7.5, 25°C, mutant C226S, co-substrate: protochlorophyllide
Thermosynechococcus elongatus
0.0118
-
protochlorophyllide
mutant C226S; pH 7.5, 25°C, mutant C226S, co-substrate: NADPH
Thermosynechococcus elongatus
0.162
-
NADPH
pH 7.5, 25°C, mutant C199S, co-substrate: protochlorophyllide
Thermosynechococcus elongatus
0.162
-
protochlorophyllide
mutant C199S; pH 7.5, 25°C, mutant C199S, co-substrate: NADPH
Thermosynechococcus elongatus
0.163
-
protochlorophyllide
mutant C37S/C199S
Thermosynechococcus elongatus
0.164
-
NADPH
pH 7.5, 25°C, mutant C37S, co-substrate: protochlorophyllide
Thermosynechococcus elongatus
0.164
-
protochlorophyllide
mutant C37S; pH 7.5, 25°C, mutant C37S, co-substrate: NADPH
Thermosynechococcus elongatus
0.165
-
NADPH
pH 7.5, 25°C, wild-type, co-substrate: protochlorophyllide
Thermosynechococcus elongatus
0.165
-
protochlorophyllide
pH 7.5, 25°C, wild-type, co-substrate: NADPH; wild type enzyme
Thermosynechococcus elongatus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
activity assay; assay at
Thermosynechococcus elongatus
Cofactor
Cofactor
Commentary
Organism
Structure
NADPH
-
Thermosynechococcus elongatus
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli; expression in Escherichia coli cells
Thermosynechococcus elongatus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADPH
-
Thermosynechococcus elongatus
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
C199/C226S
mutant, mutation of the absolutely conserved cysteine residues
Thermosynechococcus elongatus
C199S
kcat comparable to wild-type, relative activity comparable to wild-type, Kd (NADPH) comparable to wild-type, Kd (protochlorophyllide) comparable to wild-type; mutant, Cys199 has a relatively minor role in catalysis
Thermosynechococcus elongatus
C199S/C226S
kcat more that 10fold decreased to wild-type, relative activity highly decreased compared to wild-type, Kd (NADPH) 2fold increased compared to wild-type, Kd (protochlorophyllide) 6fold increased compared to wild-type
Thermosynechococcus elongatus
C226S
kcat more that 10fold decreased to wild-type, relative activity highly decreased compared to wild-type, Kd (NADPH) comparable to wild-type, Kd (protochlorophyllide) 4fold increased compared to wild-type; mutant, mutation causes a remarkable change in the mechansim of the hydrogen transfer reactions
Thermosynechococcus elongatus
C37S
kcat comparable to wild-type, relative activity comparable to wild-type, Kd (NADPH) increased compared to wild-type, Kd (protochlorophyllide) equal to wild-type; mutant, Cys37 has a relatively minor role in catalysis
Thermosynechococcus elongatus
C37S/C199S
kcat comparable to wild-type, relative activity comparable to wild-type, Kd (NADPH) 10fold increased compared to wild-type, Kd (protochlorophyllide) comparable to wild-type; mutant, mutation of the absolutely conserved cysteine residues
Thermosynechococcus elongatus
C37S/C199S/C226S
kcat more that 10fold decreased to wild-type, relative activity highly decreased compared to wild-type, Kd (NADPH) 10fold increased compared to wild-type, Kd (protochlorophyllide) 6fold increased compared to wild-type; mutant, mutation of the absolutely conserved cysteine residues
Thermosynechococcus elongatus
C37S/C226S
kcat more that 10fold decreased to wild-type, relative activity highly decreased compared to wild-type, Kd (NADPH) 10fold increased compared to wild-type, Kd (protochlorophyllide) 6fold increased compared to wild-type; mutant, mutation of the absolutely conserved cysteine residues
Thermosynechococcus elongatus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
protochlorophyllide
mutant C199/C226S, relative activity 6.6%; mutant C199S, relative activity 98.2%; mutant C226S, relative activity 7.2%; mutant C37S/C199S/C226S, relative activity 7.1%; mutant C37S/C199S, relative activity 98.8%; mutant C37S/C226S, relative activity 6.8%; mutant C37S, relative activity 99.4%; wild type enzyme, relative activity 100%
Thermosynechococcus elongatus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
protochlorophyllide + NADPH
Thermosynechococcus elongatus
-
chlorophyllide + NADP+
-
-
?
protochlorophyllide + NADPH + H+
Thermosynechococcus elongatus
activation by light
chlorophyllide + NADP+
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
protochlorophyllide + NADPH
-
699004
Thermosynechococcus elongatus
chlorophyllide + NADP+
-
-
-
?
protochlorophyllide + NADPH + H+
activation by light
699004
Thermosynechococcus elongatus
chlorophyllide + NADP+
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Thermosynechococcus elongatus
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.011
-
NADPH
pH 7.5, 25°C, mutant C199S/C226S, co-substrate: protochlorophyllide
Thermosynechococcus elongatus
0.011
-
protochlorophyllide
mutant C199/C226S; pH 7.5, 25°C, mutant C199S/C226S, co-substrate: NADPH
Thermosynechococcus elongatus
0.0113
-
NADPH
pH 7.5, 25°C, mutant C37S/C226S, co-substrate: protochlorophyllide
Thermosynechococcus elongatus
0.0113
-
protochlorophyllide
mutant C37S/C226S; pH 7.5, 25°C, mutant C37S/C226S, co-substrate: NADPH
Thermosynechococcus elongatus
0.0117
-
NADPH
pH 7.5, 25°C, mutant C37S/C199S/C226S, co-substrate: protochlorophyllide
Thermosynechococcus elongatus
0.0117
-
protochlorophyllide
mutant C37S/C199S/C226S; pH 7.5, 25°C, mutant C37S/C199S/C226S, co-substrate: NADPH
Thermosynechococcus elongatus
0.0118
-
NADPH
pH 7.5, 25°C, mutant C226S, co-substrate: protochlorophyllide
Thermosynechococcus elongatus
0.0118
-
protochlorophyllide
mutant C226S; pH 7.5, 25°C, mutant C226S, co-substrate: NADPH
Thermosynechococcus elongatus
0.162
-
NADPH
pH 7.5, 25°C, mutant C199S, co-substrate: protochlorophyllide
Thermosynechococcus elongatus
0.162
-
protochlorophyllide
mutant C199S; pH 7.5, 25°C, mutant C199S, co-substrate: NADPH
Thermosynechococcus elongatus
0.163
-
protochlorophyllide
mutant C37S/C199S
Thermosynechococcus elongatus
0.164
-
NADPH
pH 7.5, 25°C, mutant C37S, co-substrate: protochlorophyllide
Thermosynechococcus elongatus
0.164
-
protochlorophyllide
mutant C37S; pH 7.5, 25°C, mutant C37S, co-substrate: NADPH
Thermosynechococcus elongatus
0.165
-
NADPH
pH 7.5, 25°C, wild-type, co-substrate: protochlorophyllide
Thermosynechococcus elongatus
0.165
-
protochlorophyllide
pH 7.5, 25°C, wild-type, co-substrate: NADPH; wild type enzyme
Thermosynechococcus elongatus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
activity assay; assay at
Thermosynechococcus elongatus
Other publictions for EC 1.3.1.33
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)
740022
Gabruk
MGDG, PG and SQDG regulate the ...
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474
1307-1320
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1
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2
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2
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2
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2
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-
741108
Stolarik
Transcriptional and post-trans ...
Picea abies
Photosyn. Res.
132
165-179
2017
-
-
-
-
-
-
-
-
-
-
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1
-
4
-
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1
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1
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1
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1
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1
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1
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1
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-
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-
741184
Buhr
NADPH:protochlorophyllide oxid ...
Arabidopsis thaliana
Plant Mol. Biol.
94
45-59
2017
-
-
-
-
2
-
-
-
-
-
1
1
-
4
-
-
-
-
-
1
-
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1
1
-
-
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-
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1
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1
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2
-
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1
1
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1
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1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
741396
Kwon
Two NADPH: protochlorophyllide ...
Oryza sativa
Rice (N.Y.)
10
1-1
2017
-
-
-
-
-
-
-
-
-
-
-
1
-
2
-
-
-
-
-
1
-
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1
-
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1
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1
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1
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1
-
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1
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
737615
Nomata
Stoichiometry of ATP hydrolysi ...
Rhodobacter capsulatus
Biochem. Biophys. Res. Commun.
470
704-709
2016
-
-
-
-
-
-
-
-
-
-
-
1
-
2
-
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1
-
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-
-
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2
-
-
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-
-
-
-
-
3
-
-
-
-
-
-
3
-
-
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-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
740086
Hoeven
Cross-species analysis of prot ...
Chlamydomonas reinhardtii, Cyanidioschyzon merolae, Daucus carota, Lyngbya majuscula, Marchantia paleacea, Nicotiana tabacum, Nostoc punctiforme, Physcomitrella patens, Pinus mugo, Zea mays
Biochemistry
55
903-913
2016
-
-
10
-
-
-
10
20
-
-
-
10
-
13
-
-
-
-
-
-
-
-
10
-
-
-
-
10
-
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-
10
3
-
-
-
-
10
10
-
-
-
-
10
3
20
-
-
-
10
-
-
-
-
-
-
-
-
10
-
-
-
-
10
-
-
-
-
-
-
-
-
-
-
740894
Menon
Multiple active site residues ...
Thermosynechococcus elongatus
J. Photochem. Photobiol. B
161
236-243
2016
-
-
1
-
16
-
-
-
-
-
-
1
-
1
-
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-
-
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1
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6
-
-
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1
-
-
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1
1
-
16
-
-
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-
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1
-
-
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-
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-
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1
-
-
-
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6
-
-
-
-
-
-
-
-
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-
741255
Hunsperger
Differential regulation of dup ...
Phaeodactylum tricornutum
PLoS ONE
11
e0158614
2016
-
-
-
-
-
-
-
-
1
-
4
1
-
4
-
-
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-
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1
1
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1
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1
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1
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4
1
-
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1
1
-
-
-
-
-
-
-
-
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1
1
-
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-
740071
Gabruk
Light-dependent protochlorophy ...
Arabidopsis thaliana
Biochemistry
54
5255-5262
2015
-
-
-
-
-
-
-
-
2
-
-
1
-
1
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1
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1
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1
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2
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1
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1
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-
-
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-
741337
Reinbothe
Cell growth defect factor 1 is ...
Arabidopsis thaliana
Proc. Natl. Acad. Sci. USA
112
5838-5843
2015
-
-
-
-
-
-
-
-
2
-
-
1
-
6
-
-
-
-
-
1
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1
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-
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-
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1
-
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1
-
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2
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1
-
-
-
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1
-
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1
-
-
-
-
-
-
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-
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-
-
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-
741021
Kaschner
Discovery of the first light-d ...
Dinoroseobacter shibae, Dinoroseobacter shibae DFL12T
Mol. Microbiol.
93
1066-1078
2014
-
-
-
-
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2
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6
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2
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1
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1
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2
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2
-
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-
-
-
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741099
Silva
With or without light: compari ...
Rhodobacter capsulatus, Rhodobacter capsulatus ATCC BAA-309
PeerJ.
2
e551
2014
-
-
-
-
-
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2
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2
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2
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Laser excitation studies of th ...
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A plant porphyria related to d ...
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Schemenewitz
A substrate-independent, 14:3: ...
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Spectroscopic and kinetic char ...
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Characterization of three gene ...
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Nomata
Nitrogenase Fe protein-like Fe ...
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The first catalytic step of th ...
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Reinbothe
In vitro-mutagenesis of NADPH: ...
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Mol. Genet. Genomics
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Reinbothe
A role of Toc33 in the protoch ...
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Nomata
Overexpression and characteriz ...
Rhodobacter capsulatus
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Denev
Organization of protochlorophy ...
Triticum aestivum
Biochim. Biophys. Acta
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97-103
2005
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McFarlane
Kinetic characterisation of th ...
Thermosynechococcus elongatus
Photochem. Photobiol. Sci.
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1055-1059
2005
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676494
Kim
Multiplicity of different cell ...
Arabidopsis thaliana
Plant J.
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2005
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656908
Masuda
Novel insights into the enzymo ...
Amaranthus tricolor, Anabaena sp., Arabidopsis thaliana, Avena sativa, Bigelowiella natans, Chlamydomonas reinhardtii, Cucumis sativus, Daucus carota, Gloeobacter violaceus, Hordeum vulgare, Lactuca sativa, Leptolyngbya boryana, Marchantia paleacea, Nicotiana tabacum, Oryza sativa, Pinus mugo, Pinus strobus, Pinus taeda, Pisum sativum, Prochlorococcus marinus, Solanum lycopersicum, Synechocystis sp., Thermosynechococcus elongatus BP-1, Triticum aestivum, Vigna radiata
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25
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5
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16
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30
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656960
Solymosi
Hg2+ reacts with different com ...
Triticum aestivum
Plant Biol.
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358-368
2004
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657112
Reinbothe
LHPP, the light-harvesting NAD ...
Hordeum vulgare
Plant Sci.
167
1027-1041
2004
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2
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2
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657347
Antipova
-
Photoregulation of protochloro ...
Nicotiana tabacum
Russ. J. Plant Physiol.
51
152-155
2004
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1
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654705
Heyes
Protochlorophyllide oxidoreduc ...
Synechocystis sp.
Biochemistry
42
523-528
2003
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1
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1
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2
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654842
Helfrich
Chlorophylls of the c family: ...
Avena sativa
Biochim. Biophys. Acta
1605
97-103
2003
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1
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1
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2
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656854
Heyes
Ultrafast enzymatic reaction d ...
Synechocystis sp.
Nat. Struct. Biol.
10
491-492
2003
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1
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656982
Masuda
Functional analysis of isoform ...
Arabidopsis thaliana
Plant Cell Physiol.
44
963-974
2003
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1
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1
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657001
Frick
An Arabidopsis porB porC doubl ...
Arabidopsis sp.
Plant J.
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141-153
2003
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Selstam
The effects of low pH on the p ...
Avena sativa, Pisum sativum, Zea mays
Eur. J. Biochem.
269
2336-2346
2002
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3
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Pattanayak
Catalytic function of a novel ...
Arabidopsis thaliana
Biochem. Biophys. Res. Commun.
291
921-924
2002
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1
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1
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656904
Lebedev
POR structural domains importa ...
Pisum sativum
Photosyn. Res.
74
153-163
2002
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1
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656905
Masuda
Identification of two differen ...
Nicotiana tabacum
Photosyn. Res.
74
165-172
2002
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656911
Lenti
-
Mercury inhibits the activity ...
Triticum aestivum
Photosynthetica
40
145-151
2002
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393864
Lebedev
Tyr275 and Lys279 Stabilize NA ...
Pisum sativum
Biochemistry
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12562-12574
2001
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393865
Su
POR C of Arabidopsis thaliana: ...
Arabidopsis thaliana, Chlamydomonas reinhardtii, Cucumis sativus, Cucurbita pepo, Hordeum vulgare, Leptolyngbya boryana, Marchantia paleacea, Pinus mugo, Pinus strobus, Pinus taeda, Pisum sativum, Rhodobacter capsulatus
Plant Mol. Biol.
47
805-813
2001
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393861
Franck
Regulation of etioplast pigmen ...
Arabidopsis thaliana, Avena sativa
Plant Physiol.
124
1678-1696
2000
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393862
Fujita
Reconstitution of light-indepe ...
Chlamydomonas reinhardtii, Leptolyngbya boryana, Rhodobacter capsulatus
J. Biol. Chem.
275
23583-23588
2000
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393863
Heyes
NADPH:protochlorophyllide oxid ...
Chlamydomonas reinhardtii, Synechocystis sp.
FEBS Lett.
483
47-51
2000
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393858
Dahlin
The role of protein surface ch ...
Avena sativa, Chlamydomonas reinhardtii, Hordeum vulgare, Pisum sativum, Synechocystis sp., Triticum aestivum
Plant Mol. Biol.
39
309-323
1999
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393859
Klement
Pigment-free NADPH:protochloro ...
Arabidopsis thaliana, Avena sativa, Hordeum vulgare, Pisum sativum
Eur. J. Biochem.
265
862-874
1999
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393860
Lebedev
Protochlorophyllide oxidoreduc ...
Arabidopsis thaliana, Hordeum vulgare
Proc. Natl. Acad. Sci. USA
96
9954-9959
1999
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393857
Chahdi
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Isolation and characterization ...
Arabidopsis thaliana, Cucumis sativus, Hordeum vulgare, Phaseolus vulgaris, Pisum sativum, Triticum aestivum
Planta
206
673-680
1998
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393856
Martin
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Purification and kinetic analy ...
Hordeum vulgare, Pisum sativum, Tetradesmus obliquus
Biochem. J.
325
139-145
1997
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393855
Helfrich
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Absolute configuration of prot ...
Hordeum vulgare, Triticum aestivum
J. Am. Chem. Soc.
118
2606-2611
1996
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393853
Armstrong
Identification of NADPH:protoc ...
Arabidopsis thaliana, Avena sativa, Hordeum vulgare, Lepidium sativum, Pinus mugo, Pinus strobus, Pinus taeda, Pisum sativum, Triticum aestivum, Zea mays
Plant Physiol.
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1505-1517
1995
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393854
Wilks
A light-dependent complementat ...
Pisum sativum, Rhodobacter capsulatus
Proc. Natl. Acad. Sci. USA
92
724-728
1995
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393852
Darrah
Cloning and sequencing of prot ...
Avena sativa, Hordeum vulgare
Biochem. J.
265
789-798
1990
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393848
Begley
-
Protochlorophyllide reductase. ...
Avena sativa, Cucurbita pepo, Hordeum vulgare, Triticum aestivum
J. Am. Chem. Soc.
111
3095-3096
1989
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393849
Peschek
Light-independent NADPH-protoc ...
Synechococcus elongatus PCC 7942
Biochem. Biophys. Res. Commun.
162
71-78
1989
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393850
Peschek
Chlorophyll precursors in the ...
Synechococcus elongatus PCC 7942
J. Biol. Chem.
264
11827-11832
1989
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393851
Schulz
Nucleotide sequence of a cDNA ...
Arabidopsis thaliana, Hordeum vulgare, Triticum aestivum
Mol. Gen. Genet.
217
355-361
1989
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393847
Walker
-
Protochlorophyllide reductase: ...
Triticum aestivum
FEBS Lett.
239
259-262
1988
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393845
Roeper
-
Amino acid composition of the ...
Avena sativa
Plant Sci.
52
15-19
1987
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393846
Valera
Synthesis of 4R- and 4S-tritiu ...
Triticum aestivum
Biochem. Biophys. Res. Commun.
148
515-520
1987
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393843
Dehesh
Light-induced changes in the d ...
Avena sativa, Cucurbita pepo, Hordeum vulgare, Triticum aestivum
Planta
169
162-171
1986
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393844
Dehesh
Light-induced changes in the d ...
Hordeum vulgare, Secale cereale, Triticum aestivum, Zea mays
Planta
169
172-183
1986
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393842
Dehesh
The NADPH-protochlorophyllide ...
Hordeum vulgare, Phaseolus vulgaris, Triticum aestivum
Planta
164
396-399
1985
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393841
Haeuser
The proteolytic degradation in ...
Avena sativa, Hordeum vulgare
Arch. Biochem. Biophys.
228
577-586
1984
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393840
Ford
-
Characterization of NADPH: Pro ...
Chlamydomonas reinhardtii
Mol. Gen. Genet.
192
290-292
1983
1
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393839
Griffiths
Site of synthesis of NADPH pro ...
Avena sativa, Hordeum vulgare, Secale cereale
Plant Physiol.
70
1014-1018
1982
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393836
Beer
Purification of the enzyme NAD ...
Avena sativa, Hordeum vulgare, Phaseolus vulgaris
Biochem. J.
195
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1981
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393837
Luetz
Sub-etioplast localization of ...
Avena sativa
Eur. J. Biochem.
118
347-353
1981
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393838
Oliver
Covalent labelling of the NADP ...
Avena sativa, Hordeum vulgare, Phaseolus vulgaris
Biochem. J.
195
93-101
1981
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3
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393833
Apel
The protochlorophyllide holoch ...
Hordeum vulgare
Eur. J. Biochem.
111
251-258
1980
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-
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1
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3
-
1
1
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2
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1
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1
1
1
1
1
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3
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1
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1
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1
1
1
1
1
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393834
Griffiths
Substrate-specificity studies ...
Hordeum vulgare
Biochem. J.
186
267-278
1980
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-
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3
2
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2
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2
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3
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1
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3
2
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2
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1
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3
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393835
Oliver
Identification of the polypept ...
Avena sativa
Biochem. J.
191
277-280
1980
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-
-
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2
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1
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2
1
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1
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1
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1
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2
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1
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2
1
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1
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1
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393832
Griffiths
Reconstitution of chlorophylli ...
Hordeum vulgare
Biochem. J.
174
681-692
1978
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2
1
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1
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1
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1
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1
1
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1
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