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• W2000422571 abstract "Thermodynamically unfavourable electron transfers are enabled by coupling to an energy-supplying reaction. How the energy is transduced from the exergonic to the endergonic process is largely unknown. Here we provide the structural basis for an energy transduction process in the reductive activation of B12-dependent methyltransferases. The transfer of one electron from an activating enzyme to the cobalamin cofactor is energetically uphill and relies on coupling to an ATPase reaction. Our results demonstrate that the key to coupling is, besides the oxidation state-dependent complex formation, the conformational gating of the electron transfer. Complex formation induces a substitution of the ligand at the electron-accepting Co ion. Addition of ATP initiates electron transfer by provoking conformational changes that destabilize the complex. We show how remodelling of the electron-accepting Co2+ promotes ATP-dependent electron transfer; an efficient strategy not seen in other electron-transferring ATPases. Some biological reactions can require thermodynamically unfavourable electron transfer processes, the occurrence of which are not yet fully understood. Here, the authors provide the structural basis of energy transduction during the reductive activation of B12-dependent methyltransferases." @default.
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• W2000422571 date "2014-08-11" @default.
• W2000422571 modified "2023-10-02" @default.
• W2000422571 title "ATP-induced electron transfer by redox-selective partner recognition" @default.
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• W2000422571 doi "https://doi.org/10.1038/ncomms5626" @default.
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