The crystal structure of catechol oxidase: new insight into the function of type-3 copper proteins

Acc Chem Res. 2002 Mar;35(3):183-91. doi: 10.1021/ar990019a.

Abstract

The crystal structure of catechol oxidase reveals new insight into the functional properties of the type-3 copper proteins. This class of proteins includes the closely related and better-known tyrosinase as well as hemocyanin, an oxygen transport protein. All these proteins have a dinuclear copper center, have similar spectroscopic behaviors, and show close evolutionary and functional relationships. Comparison between the 3D structures of catechol oxidase and hemocyanins reveals the structural reasons for the divergence in function.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Catechol Oxidase / chemistry*
  • Catechol Oxidase / metabolism
  • Catechol Oxidase / physiology
  • Copper / chemistry*
  • Crystallization
  • Hemocyanins / chemistry
  • Metalloproteins / chemistry
  • Oxidation-Reduction
  • Plant Proteins / chemistry
  • Plant Proteins / metabolism
  • Plant Proteins / physiology
  • Protein Conformation
  • Sequence Alignment
  • Structure-Activity Relationship

Substances

  • Metalloproteins
  • Plant Proteins
  • Copper
  • Hemocyanins
  • Catechol Oxidase