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Literature summary for 1.8.7.1 extracted from

  • Kim, J.Y.; Nakayama, M.; Toyota, H.; Kurisu, G.; Hase, T.
    Structural and mutational studies of an electron transfer complex of maize sulfite reductase and ferredoxin (2016), J. Biochem., 160, 101-109 .
    View publication on PubMed
Search for more literature for 1.8.7.1

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Zea mays

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Protein Variants

Protein Variants Comment Organism
A493G mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity Zea mays
A503G mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity Zea mays
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
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
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
L499G mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity Zea mays
L502A mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity Zea mays
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
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
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
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
P501G mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity Zea mays
P541G mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity Zea mays
Q504G mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity Zea mays

Organism

Organism UniProt Comment Textmining
Zea mays O23813
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
hydrogen sulfide + oxidized ferredoxin + H2O
-
 Zea mays sulfite + reduced ferredoxin + H+
-
 ?
hydrogen sulfide + oxidized methyl viologen + H2O
-
 Zea mays sulfite + reduced methyl viologen + H+
-
 ?

Cofactor

Cofactor Comment Organism Structure
[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