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Structural evidence for asymmetrical nucleotide interactions in nitrogenase.

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New nitrogenase structures reveal asymmetric nucleotide binding, suggesting ATP hydrolysis occurs stepwise. This mechanism may control electron transfer for nitrogen fixation.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • The nitrogenase complex catalyzes essential nitrogen fixation.
  • The precise role of adenosine triphosphate (ATP) hydrolysis in its electron-transfer (ET) reactions is not fully understood.

Purpose of the Study:

  • To elucidate the mechanism of ATP hydrolysis in the nitrogenase catalytic cycle.
  • To investigate the structural basis for nucleotide binding and its impact on enzyme function.

Main Methods:

  • Crystallization of the nitrogenase complex with MgADP and MgAMPPCP (an ATP analogue).
  • X-ray crystallography to determine the high-resolution structure of the complex.

Main Results:

  • A novel structure of the nitrogenase complex was determined, showing asymmetric binding of two nucleotides (MgADP and MgAMPPCP) to the Fe-protein subunits.
  • These nucleotides were associated with two different MoFe-protein subunits, indicating a non-symmetrical interaction.

Conclusions:

  • The asymmetric nucleotide binding suggests a stepwise mechanism for ATP hydrolysis and phosphate release.
  • This stepwise process, coupled with Fe-protein conformational changes, likely prolongs the Fe-protein-MoFe-protein complex's lifetime.
  • This prolonged interaction may orchestrate the sequential intracomplex electron transfer crucial for substrate reduction in nitrogen fixation.