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Matches in SemOpenAlex for { <https://semopenalex.org/work/W1987483478> ?p ?o ?g. }

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• W1987483478 startingPage "3247" @default.
• W1987483478 abstract "We have characterized by EPR the interaction of the Em,7 = -50 mV [4Fe-4S] cluster of Escherichia coli DMSO reductase (DmsABC) with a menaquinol (MQH2) binding site. Potentiometric titrations indicate that in DmsAB(C102S)C, the Em,7 = -50 mV [4Fe-4S] cluster is replaced by an Em,7 = +260 mV [3Fe-4S] cluster. The Q-pool coupling assay in combination with the MQH2 analog HOQNO (2-n-heptyl-4-hydroxyquinoline-N-oxide) was used to examine the effect of the DmsB(Cl02S) mutation on physiological electron transfer through DmsABC. Forward electron transfer through the mutant (MQH2 to DmsA) is blocked in the Q-pool coupling assay, but reverse electron transfer (DmsA to MQ) is not. HOQNO elicits a significant change in the EPR line shape of the oxidized DmsAB(Cl02S)C [3Fe-4S] cluster but has no effect on the line shape of the reduced [4Fe-4S] clusters. We have identified a residue in DmsC involved in MQH2 oxidation. DmsC(H65), and in a double mutant, DmsAB(C102S)C(H65R), the DmsC mutation blocks the HOQNO effect on the [3Fe-4S] EPR line shape, suggesting, that the DmsC(H65R) mutation either blocks HOQNO binding or blocks a conformational link between a HOQNO binding site and the DmsB(C102S) [3Fe-4S] cluster. These results suggest that the MQH2 binding site of DmsC is conformationally and functionally linked to the Em,7 = -50 mV [4Fe-4S] cluster of DmsB." @default.
• W1987483478 created "2016-06-24" @default.
• W1987483478 creator A5026785330 @default.
• W1987483478 creator A5040629503 @default.
• W1987483478 date "1996-01-01" @default.
• W1987483478 modified "2023-09-26" @default.
• W1987483478 title "Interaction of an Engineered [3Fe-4S] Cluster with a Menaquinol Binding Site of <i>Escherichia coli</i> DMSO Reductase" @default.
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• W1987483478 doi "https://doi.org/10.1021/bi951584y" @default.
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