BRENDA - Enzyme Database show
show all sequences of 1.8.7.1

A new type of sulfite reductase, a novel coenzyme F420-dependent enzyme, from the methanarchaeon Methanocaldococcus jannaschii

Johnson, E.F.; Mukhopadhyay, B.; J. Biol. Chem. 280, 38776-38786 (2005)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
coenzyme F420
-
Methanocaldococcus jannaschii
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0122
-
sulfite
within a sulfite concentration range of 0.0014-0.3 mM and with a fixed reduced coenzyme F420 concentration of 0.04 mM
Methanocaldococcus jannaschii
0.021
-
reduced coenzyme F420
at a fixed sulfite concentration of 0.29 mM and within a reduced coenzyme F420 concentration range of 0.004-0.06 mM
Methanocaldococcus jannaschii
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
70000
-
SDS-PAGE
Methanocaldococcus jannaschii
350000
-
gel filtration
Methanocaldococcus jannaschii
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Methanocaldococcus jannaschii
-
-
-
Purification (Commentary)
Commentary
Organism
phenyl-Sepharose chromatography, F420-Sepharose chromatography and QAE-Sephadex gel filtration
Methanocaldococcus jannaschii
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.0013
-
in 50 mM potassium phosphate buffer (pH 7), 0.044 mM reduced coenzyme F420, and 1.5 mM sodium sulfite, from cell extract
Methanocaldococcus jannaschii
0.0182
-
in 50 mM potassium phosphate buffer (pH 7), 0.044 mM reduced coenzyme F420, and 1.5 mM sodium sulfite, after 14fold purification
Methanocaldococcus jannaschii
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
sulfite + reduced coenzyme F420
-
674504
Methanocaldococcus jannaschii
sulfide + oxidized coenzyme F420
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
95
-
-
Methanocaldococcus jannaschii
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
-
Methanocaldococcus jannaschii
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
coenzyme F420
-
Methanocaldococcus jannaschii
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0122
-
sulfite
within a sulfite concentration range of 0.0014-0.3 mM and with a fixed reduced coenzyme F420 concentration of 0.04 mM
Methanocaldococcus jannaschii
0.021
-
reduced coenzyme F420
at a fixed sulfite concentration of 0.29 mM and within a reduced coenzyme F420 concentration range of 0.004-0.06 mM
Methanocaldococcus jannaschii
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
70000
-
SDS-PAGE
Methanocaldococcus jannaschii
350000
-
gel filtration
Methanocaldococcus jannaschii
Purification (Commentary) (protein specific)
Commentary
Organism
phenyl-Sepharose chromatography, F420-Sepharose chromatography and QAE-Sephadex gel filtration
Methanocaldococcus jannaschii
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.0013
-
in 50 mM potassium phosphate buffer (pH 7), 0.044 mM reduced coenzyme F420, and 1.5 mM sodium sulfite, from cell extract
Methanocaldococcus jannaschii
0.0182
-
in 50 mM potassium phosphate buffer (pH 7), 0.044 mM reduced coenzyme F420, and 1.5 mM sodium sulfite, after 14fold purification
Methanocaldococcus jannaschii
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
sulfite + reduced coenzyme F420
-
674504
Methanocaldococcus jannaschii
sulfide + oxidized coenzyme F420
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
95
-
-
Methanocaldococcus jannaschii
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
-
Methanocaldococcus jannaschii
Other publictions for EC 1.8.7.1
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)
742810
Sekine
Characterization of two ferre ...
Cyanidioschyzon merolae 10D, Cyanidioschyzon merolae
J. Biochem.
162
37-43
2017
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1
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3
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1
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2
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741859
Kim
Non-covalent forces tune the ...
Zea mays
Biochem. J.
473
3837-3854
2016
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1
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1
1
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742806
Kim
Structural and mutational stu ...
Zea mays
J. Biochem.
160
101-109
2016
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1
1
14
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14
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2
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726232
Yarmolinsky
Sulfite reductase protects pla ...
Arabidopsis thaliana, Solanum lycopersicum
Plant Physiol.
161
725-743
2013
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6
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10
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2
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2
2
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726121
McManus
Genotypic variation in sulfur ...
Allium cepa
Phytochemistry
83
34-42
2012
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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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726144
Brychkova
A novel in-gel assay and an im ...
Arabidopsis thaliana, Solanum lycopersicum
Plant Cell Physiol.
53
1507-1516
2012
4
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8
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2
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726184
Kang
In vivo effects of NbSiR silen ...
Nicotiana benthamiana
Plant Mol. Biol.
72
569-583
2010
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1
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1
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1
1
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2
2
-
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696126
Sekine
A novel variant of ferredoxin- ...
Cyanidioschyzon merolae
Biochem. J.
423
91-98
2009
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1
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2
2
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1
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1
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1
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3
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2
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1
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688412
Schiffer
Structure of the dissimilatory ...
Archaeoglobus fulgidus
J. Mol. Biol.
379
1063-1074
2008
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1
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686650
Sekine
DNA binding and partial nucleo ...
Pisum sativum, Zea mays
FEBS J.
274
2054-2069
2007
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674525
Saitoh
NMR study of the electron tran ...
Zea mays
J. Biol. Chem.
281
10482-10488
2006
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1
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4
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1
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3
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4
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674459
Schnell
Siroheme- and [Fe4-S4]-depende ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
J. Biol. Chem.
280
27319-27328
2005
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1
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674504
Johnson
A new type of sulfite reductas ...
Methanocaldococcus jannaschii
J. Biol. Chem.
280
38776-38786
2005
1
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1
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676333
Hirasawa
Chemical modification studies ...
Zea mays
Photosyn. Res.
86
325-336
2005
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3
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2
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2
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437707
Chi-Ham
The DNA-compacting protein DCP ...
Glycine max, Pisum sativum
Plant Mol. Biol.
49
621-631
2002
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3
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2
1
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3
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657926
Champier
Reactivity, secondary structur ...
Escherichia coli
Biochemistry
41
3770-3780
2002
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1
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437706
Yonekura-Sakakibara
Analysis of reductant supply s ...
Zea mays
Plant Physiol.
122
887-894
2000
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437705
Akashi
Comparison of the electrostati ...
Zea mays
J. Biol. Chem.
274
29399-29405
1999
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3
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437704
Takahashi
Purification and characterizat ...
Brassica rapa
Biosci. Biotechnol. Biochem.
61
1486-1490
1997
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1
4
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1
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1
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4
1
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4
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1
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1
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1
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1
4
1
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437701
Takahashi
-
Effect of sulfur and nitrogen ...
Allium tuberosum
J. Plant Res.
109
363-368
1996
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1
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1
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437702
Takahashi
-
Purification and characterizat ...
Allium tuberosum
J. Plant Res.
109
45-52
1996
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2
1
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1
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1
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437703
Takahashi
-
Ferredoxin-linked sulfite redu ...
Brassica rapa, Spinacia oleracea
Biosci. Biotechnol. Biochem.
60
142-144
1996
-
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1
2
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2
2
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2
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1
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1
1
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1
1
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1
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2
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2
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1
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2
2
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1
-
1
1
-
2
1
1
-
-
-
1
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-
437687
Koguchi
-
Isolation and partial characte ...
Pyropia yezoensis
Agric. Biol. Chem.
53
1653-1662
1989
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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
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1
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1
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1
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1
1
-
1
1
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-
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-
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-
437691
Brunold
Localization of enzymes of ass ...
Pisum sativum
Planta
179
228-234
1989
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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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-
437692
Koguchi
-
Reduction of S-sulfoglutathion ...
Arthrospira platensis, Arthrospira platensis OU-1
Agric. Biol. Chem.
53
783-788
1989
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-
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2
2
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1
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3
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1
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4
1
1
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1
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2
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2
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1
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1
-
4
1
1
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-
-
1
-
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-
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-
-
-
-
437688
Koguchi
-
Purification and partial chara ...
Brassica rapa subsp. chinensis
Agric. Biol. Chem.
52
1867-1868
1988
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-
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2
1
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1
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1
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1
1
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2
1
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1
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1
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2
1
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1
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1
1
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2
1
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-
-
-
-
437689
Koguchi
-
Ferredoxin-sulfite reductase f ...
Arthrospira platensis, Arthrospira platensis OU-1
Agric. Biol. Chem.
52
373-380
1988
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-
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1
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2
2
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3
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1
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1
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2
1
1
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1
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1
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1
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2
2
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1
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1
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2
1
1
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-
437693
Hirasawa
-
The interaction of ferredoxin- ...
Spinacia oleracea
FEBS Lett.
221
343-348
1987
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-
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-
-
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2
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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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2
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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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437694
Krueger
Evidence for siroheme-Fe4S4 in ...
Pisum sativum, Spinacia oleracea
Biochemistry
21
2905-2909
1982
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-
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1
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3
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1
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1
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437695
Krueger
Spinach siroheme enzymes: Isol ...
Spinacia oleracea
Biochemistry
21
2892-2904
1982
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-
-
-
-
-
-
6
-
1
4
1
-
3
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1
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2
-
2
1
1
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1
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1
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-
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6
-
1
4
1
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1
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2
-
2
1
1
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437690
Aketagawa
Ferredoxin-sulfite reductase f ...
Spinacia oleracea
Agric. Biol. Chem.
44
2371-2378
1980
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-
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4
1
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1
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1
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1
1
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1
1
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1
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1
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4
1
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1
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1
1
-
1
1
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-
-
-
-
437696
Hall
EPR spectroscopy of the iron-s ...
Desulfovibrio gigas, Desulfovibrio gigas No. 9332
Biochim. Biophys. Acta
581
27-33
1979
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1
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2
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3
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2
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1
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1
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1
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2
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2
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437697
Tamura
-
The occurrence of ferredoxin-s ...
Hordeum vulgare
Agric. Biol. Chem.
43
1601-1602
1979
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-
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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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1
-
1
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1
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-
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-
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-
437698
Tamura
Ferredoxin-dependent sulfite r ...
Spinacia oleracea
Agric. Biol. Chem.
42
2165-2167
1978
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-
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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
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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
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1
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1
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437699
Asada
-
Methyl viologen- and ferredoxi ...
Spinacia oleracea
Methods Enzymol.
17B
528-539
1971
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-
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-
1
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1
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1
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1
1
1
1
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1
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1
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1
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1
1
1
1
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-
1
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-
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-
437700
Laishley
A ferredoxin-linked sulfite re ...
Clostridium pasteurianum, Clostridium pasteurianum W5
Can. J. Microbiol.
17
889-895
1971
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2
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9
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1
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6
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1
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2
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1
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6
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1
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