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Literature summary extracted from

  • Cheng, V.W.; Rothery, R.A.; Bertero, M.G.; Strynadka, N.C.; Weiner, J.H.
    Investigation of the environment surrounding iron-sulfur cluster 4 of Escherichia coli dimethylsulfoxide reductase (2005), Biochemistry, 44, 8068-8077.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.8.5.3 C102S mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster. The midpoint potential of FS4[3Fe-4S] is insensitive to inhibitor 2-n-heptyl-4-hydroxyquinoline N-oxide as well as to changes in pH from 5 to 7 Escherichia coli
1.8.5.3 D95A mutation in electron transfer subunit DmsB Escherichia coli
1.8.5.3 D95A/C102S mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster Escherichia coli
1.8.5.3 D95K/C102S mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster Escherichia coli
1.8.5.3 D97A mutation in electron transfer subunit DmsB Escherichia coli
1.8.5.3 D97A/C102S mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster Escherichia coli
1.8.5.3 H106A mutation in electron transfer subunit DmsB Escherichia coli
1.8.5.3 H106A/C102S mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster Escherichia coli
1.8.5.3 H106E mutation in electron transfer subunit DmsB Escherichia coli
1.8.5.3 H106E/C102S mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster Escherichia coli
1.8.5.3 H106I/C102S 2 mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster Escherichia coli
1.8.5.3 H85F mutation in electron transfer subunit DmsB Escherichia coli
1.8.5.3 H85F/C102S mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster Escherichia coli
1.8.5.3 H85T mutation in electron transfer subunit DmsB Escherichia coli
1.8.5.3 H85T/C102S mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster Escherichia coli
1.8.5.3 K77A mutation in electron transfer subunit DmsB Escherichia coli
1.8.5.3 K77A/C102S mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster Escherichia coli
1.8.5.3 P80A mutation in electron transfer subunit DmsB Escherichia coli
1.8.5.3 P80A/C102S mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster Escherichia coli
1.8.5.3 P80D mutation in electron transfer subunit DmsB Escherichia coli
1.8.5.3 P80H mutation in electron transfer subunit DmsB Escherichia coli
1.8.5.3 R103A mutation in electron transfer subunit DmsB Escherichia coli
1.8.5.3 R103A/C102S mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster Escherichia coli
1.8.5.3 S81G mutation in electron transfer subunit DmsB Escherichia coli
1.8.5.3 S81H mutation in electron transfer subunit DmsB Escherichia coli
1.8.5.3 Y104A mutation in electron transfer subunit DmsB Escherichia coli
1.8.5.3 Y104A/C102S mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster Escherichia coli
1.8.5.3 Y104D mutation in electron transfer subunit DmsB Escherichia coli
1.8.5.3 Y104D/C102S mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster. Mutant dramatically lower s the midpoint potential of iron-sulfur centre FS4[3Fe-4S] from 275 to 150 mV. The midpoint potential of FS4 increases in the presence of 2-n-heptyl-4-hydroxyquinoline N-oxide and decreasing pH Escherichia coli
1.8.5.3 Y104D/H106F/C102S mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster Escherichia coli
1.8.5.3 Y104E  mutation in electron transfer subunit DmsB Escherichia coli
1.8.5.3 Y104E/C102S mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster. Mutant dramatically lower s the midpoint potential of iron-sulfur centre FS4[3Fe-4S] from 275 to 145 mV Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.8.5.3 2-n-heptyl-4-hydroxyquinoline N-oxide residues Pro80, Ser81, Cys102, and Tyr104 of electron transfer subunit DmsB are located at the DmsB-DmsC interface and are critical for the binding of the MQH2 inhibitor analogue 2-n-heptyl-4-hydroxyquinoline N-oxide Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
1.8.5.3 Escherichia coli
-
-
-

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.5.3 Fe-S center residues Pro80, Ser81, Cys102, and Tyr104 of electron transfer subunit DmsB are located at the DmsB-DmsC interface and are critical for the transfer of electrons from MQH2 to iron-sulfur cluster FS4 Escherichia coli