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Literature summary for 1.8.5.3 extracted from

  • Rothery, R.A.; Trieber, C.A.; Weiner, J.H.
    Interactions between the molybdenum cofactor and iron-sulfur clusters of Escherichia coli dimethylsulfoxide reductase (1999), J. Biol. Chem., 274, 13002-13009.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
C38S the spin-spin interaction between the reduced [4Fe-4S] cluster of subunit DmsB and the Mo(V) of the molybdo bis(molybdopterin guanine dinucleotide) cofactor of subunit DmsA is significantly modified in DmsA-C38S mutant that contains a [3Fe-4S] cluster in DmsA. In ferricyanide-oxidized glycerol-inhibited DmsAC38SBC, there is no detectable interaction between the oxidized [3Fe-4S] cluster and the molybdo bis(molybdopterin guanine dinucleotide) cofactor Escherichia coli
R77S DmsA-R77S mutant, the spin-spin interaction between the reduced [4Fe-4S] cluster of subunit DmsB and the Mo(V) of the molybdo bis(molybdopterin guanine dinucleotide) cofactor of subunit DmsA is eliminated Escherichia coli
S176A/C102S double mutant DmsA-S176A and DmsB-C102S, contains an engineered [3Fe-4S] cluster in DmsB, no significant paramagnetic interaction is detected between the oxidized [3Fe-4S] cluster and the Mo(V) Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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Cofactor

Cofactor Comment Organism Structure
Fe-S center significant spin-spin interaction between the reduced [4Fe-4S] cluster of subunit DmsB and the Mo(V) of the Mo-bisMGD of subunit DmsA. This interaction is significantly modified in a DmsA-C38S mutant that contains a [3Fe-4S] cluster in DmsA Escherichia coli
molybdopterin guanine dinucleotide
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Escherichia coli