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Literature summary for 1.8.5.3 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
Search for more literature for 1.8.5.3

Protein Variants

Protein Variants Comment Organism
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
D95A mutation in electron transfer subunit DmsB Escherichia coli
D95A/C102S mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster Escherichia coli
D95K/C102S mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster Escherichia coli
D97A mutation in electron transfer subunit DmsB Escherichia coli
D97A/C102S mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster Escherichia coli
H106A mutation in electron transfer subunit DmsB Escherichia coli
H106A/C102S mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster Escherichia coli
H106E mutation in electron transfer subunit DmsB Escherichia coli
H106E/C102S mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster Escherichia coli
H106I/C102S 2 mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster Escherichia coli
H85F mutation in electron transfer subunit DmsB Escherichia coli
H85F/C102S mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster Escherichia coli
H85T mutation in electron transfer subunit DmsB Escherichia coli
H85T/C102S mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster Escherichia coli
K77A mutation in electron transfer subunit DmsB Escherichia coli
K77A/C102S mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster Escherichia coli
P80A mutation in electron transfer subunit DmsB Escherichia coli
P80A/C102S mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster Escherichia coli
P80D mutation in electron transfer subunit DmsB Escherichia coli
P80H mutation in electron transfer subunit DmsB Escherichia coli
R103A mutation in electron transfer subunit DmsB Escherichia coli
R103A/C102S mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster Escherichia coli
S81G mutation in electron transfer subunit DmsB Escherichia coli
S81H mutation in electron transfer subunit DmsB Escherichia coli
Y104A mutation in electron transfer subunit DmsB Escherichia coli
Y104A/C102S mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster Escherichia coli
Y104D mutation in electron transfer subunit DmsB Escherichia coli
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
Y104D/H106F/C102S mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster Escherichia coli
Y104E  mutation in electron transfer subunit DmsB Escherichia coli
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

Inhibitors Comment Organism Structure
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

Organism UniProt Comment Textmining
Escherichia coli
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Cofactor

Cofactor Comment Organism Structure
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