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Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.7.1 expression in Escherichia coli Zea mays

Crystallization (Commentary)

EC Number Crystallization (Comment) 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

Protein Variants

EC Number Protein Variants Comment 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 UniProt Comment Textmining
1.8.7.1 Zea mays O23813
-
-

Substrates and Products (Substrate)

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

Cofactor

EC Number Cofactor Comment 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