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Structural and mutational studies of an electron transfer complex of maize sulfite reductase and ferredoxin

Kim, J.Y.; Nakayama, M.; Toyota, H.; Kurisu, G.; Hase, T.; J. Biochem. 160, 101-109 (2016)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Commentary
Organism
1.8.7.1
expression in Escherichia coli
Zea mays
Crystallization (Commentary)
EC Number
Crystallization
Organism
1.8.7.1
complex of maize sulfite reductase SiR and ferredoxin. A few negative residues of ferredoxin contact with a narrow area of SiR with positive electrostatic surface potential. The [2Fe-2S] cluster of ferredoxin and the [4Fe-4S] cluster of SiR are in a close proximity
Zea mays
Engineering
EC Number
Amino acid exchange
Commentary
Organism
1.8.7.1
A493G
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity
Zea mays
1.8.7.1
A503G
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity
Zea mays
1.8.7.1
Arg111Q
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme
Zea mays
1.8.7.1
Arg114Q
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme
Zea mays
1.8.7.1
Arg324Q
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme
Zea mays
1.8.7.1
L499G
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity
Zea mays
1.8.7.1
L502A
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity
Zea mays
1.8.7.1
Lys117Q
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme
Zea mays
1.8.7.1
Lys582Q
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme
Zea mays
1.8.7.1
Lys584Q
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme
Zea mays
1.8.7.1
Lys66Q
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme
Zea mays
1.8.7.1
P501G
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity
Zea mays
1.8.7.1
P541G
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity
Zea mays
1.8.7.1
Q504G
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity
Zea mays
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.8.7.1
Zea mays
O23813
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.8.7.1
hydrogen sulfide + oxidized ferredoxin + H2O
-
742806
Zea mays
sulfite + reduced ferredoxin + H+
-
-
-
?
1.8.7.1
hydrogen sulfide + oxidized methyl viologen + H2O
-
742806
Zea mays
sulfite + reduced methyl viologen + H+
-
-
-
?
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.8.7.1
[4Fe-4S]-center
in cocrystals, the [2Fe-2S] cluster of ferredoxin and the [4Fe-4S] cluster of SiR are in a close proximity
Zea mays
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
1.8.7.1
expression in Escherichia coli
Zea mays
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.8.7.1
[4Fe-4S]-center
in cocrystals, the [2Fe-2S] cluster of ferredoxin and the [4Fe-4S] cluster of SiR are in a close proximity
Zea mays
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
1.8.7.1
complex of maize sulfite reductase SiR and ferredoxin. A few negative residues of ferredoxin contact with a narrow area of SiR with positive electrostatic surface potential. The [2Fe-2S] cluster of ferredoxin and the [4Fe-4S] cluster of SiR are in a close proximity
Zea mays
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
1.8.7.1
A493G
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity
Zea mays
1.8.7.1
A503G
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity
Zea mays
1.8.7.1
Arg111Q
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme
Zea mays
1.8.7.1
Arg114Q
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme
Zea mays
1.8.7.1
Arg324Q
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme
Zea mays
1.8.7.1
L499G
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity
Zea mays
1.8.7.1
L502A
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity
Zea mays
1.8.7.1
Lys117Q
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme
Zea mays
1.8.7.1
Lys582Q
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme
Zea mays
1.8.7.1
Lys584Q
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme
Zea mays
1.8.7.1
Lys66Q
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme
Zea mays
1.8.7.1
P501G
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity
Zea mays
1.8.7.1
P541G
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity
Zea mays
1.8.7.1
Q504G
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity
Zea mays
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.8.7.1
hydrogen sulfide + oxidized ferredoxin + H2O
-
742806
Zea mays
sulfite + reduced ferredoxin + H+
-
-
-
?
1.8.7.1
hydrogen sulfide + oxidized methyl viologen + H2O
-
742806
Zea mays
sulfite + reduced methyl viologen + H+
-
-
-
?