Effects of the protein environment on the structure and energetics of active sites of metalloenzymes. ONIOM study of methane monooxygenase and ribonucleotide reductase

J Am Chem Soc. 2002 Jan 16;124(2):192-3. doi: 10.1021/ja016589z.

Abstract

As the first application of our recently developed ONIOM2(QM:MM) and ONIOM3(QM:QM:MM) codes to the metalloenzymes with a large number of protein residues, two members of the non-heme protein family, methane monooxygenause and ribonucleotide reductase, have been chosen. The "active-site + four alpha-helical fragments" model was adopted which includes about 1000 atoms from 62 residues around the Fe-centered spheres. Comparison of the active-site geometries of MMOH and R2 units optimized with this model with those obtained with the "active site only" (with only 39-46 atoms) model and the X-ray results clearly demonstrates the crucial role of the active site-protein interaction in the enzymatic activities.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Binding Sites
  • Oxygenases / chemistry*
  • Oxygenases / metabolism*
  • Protein Conformation
  • Ribonucleotide Reductases / chemistry*
  • Ribonucleotide Reductases / metabolism*

Substances

  • Oxygenases
  • methane monooxygenase
  • Ribonucleotide Reductases