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Multicopper oxidases: intramolecular electron transfer and O2 reduction.

Scot Wherland1, Ole Farver, Israel Pecht

  • 1Department of Chemistry, Washington State University, Pullman, WA, 99164-4630, USA, scot_wherland@wsu.edu.

Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry
|January 17, 2014
PubMed
Summary

Multicopper oxidases are enzymes that convert O2 to water. This review details electron transfer kinetics and intermediates in oxygen reduction by these enzymes.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Bioinorganic Chemistry

Background:

  • Multicopper oxidases are enzymes catalyzing O2 reduction to water.
  • These enzymes utilize copper binding sites for redox reactions.
  • Over 40 years of research have elucidated their structure and properties.

Purpose of the Study:

  • To review the kinetics of internal electron transfer in multicopper oxidases.
  • To explore the nature of intermediates formed during oxygen reduction.
  • To provide a detailed picture of copper binding sites' function.

Main Methods:

  • Literature review focusing on kinetic studies.
  • Analysis of structural and property data of copper binding sites.
  • Examination of intermediates in oxygen reduction pathways.

Main Results:

  • Detailed understanding of electron transfer between type 1 copper and trinuclear centers.
  • Characterization of key intermediates in the oxygen reduction mechanism.
  • Emerging detailed picture of copper site function in catalysis.

Conclusions:

  • Multicopper oxidases play a vital role in oxygen reduction.
  • Internal electron transfer kinetics are crucial for enzyme function.
  • Further research continues to refine our understanding of these complex enzymes.