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Energy transfer powers unfavorable electron transfer in methyltransferases. ATP binding triggers conformational changes, enabling electron transfer via structural remodeling of the cobalt ion.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Electron transfer reactions are fundamental in biological processes.
  • Coupling energetically unfavorable reactions to energy-releasing ones is crucial for biological function.
  • The mechanism of energy transduction in enzyme-catalyzed reactions remains incompletely understood.

Purpose of the Study:

  • To elucidate the structural basis of energy transduction in the reductive activation of B12-dependent methyltransferases.
  • To understand how an ATPase reaction energetically supports an uphill electron transfer.
  • To identify the key molecular events enabling this coupled process.

Main Methods:

  • X-ray crystallography to determine protein structures.
  • Biochemical assays to measure electron transfer rates.
  • Enzyme kinetics to analyze reaction mechanisms.
  • Mutagenesis studies to probe protein function.

Main Results:

  • Complex formation between the activating enzyme and the B12 cofactor is essential.
  • Electron transfer is gated by conformational changes induced by complex formation.
  • ATP binding triggers destabilization of the complex and initiates electron transfer.
  • Structural remodeling of the cobalt ion in the cobalamin cofactor is critical for ATP-dependent electron transfer.

Conclusions:

  • The study reveals a novel mechanism for energy transduction involving conformational gating and structural remodeling.
  • This mechanism efficiently couples ATP hydrolysis to an energetically unfavorable electron transfer.
  • The findings provide insights into the regulation of B12-dependent methyltransferases and related enzymes.
  • This strategy of ATP-dependent electron transfer is unique among known electron-transferring ATPases.