Standard Article

Copper Proteins with Type 1 Sites

  1. P. John Hart1,
  2. Aram. M. Nersissian2,
  3. Serena DeBeer George3

Published Online: 15 MAR 2006

DOI: 10.1002/0470862106.ia056

Encyclopedia of Inorganic Chemistry

Encyclopedia of Inorganic Chemistry

How to Cite

Hart, P. J., Nersissian, A. M. and George, S. D. 2006. Copper Proteins with Type 1 Sites . Encyclopedia of Inorganic Chemistry. .

Author Information

  1. 1

    University of Texas, Health Science Center, San Antonio, TX, USA

  2. 2

    Occidental College, Los Angeles, CA, USA

  3. 3

    Stanford University, Stanford, CA, USA

Publication History

  1. Published Online: 15 MAR 2006


Copper Proteins with Type 1 Sites is a general review that focuses on single-domain proteins that bind ‘blue’ or ‘type 1’ copper. Larger, multidomain proteins that contain type 1 copper in addition to other types of copper centers are not discussed at any length in this article. Blue copper proteins are so named because in solution they are a brilliant blue/azure color when the copper ion is in its Cu(II) oxidation state. The bright blue color comes from a charge transfer (CT) between Cu(II) and the sulfur (thiolate) of a ligating cysteine residue. Because of this intense color, type 1 copper proteins were among the first to be isolated because they could be tracked easily during purification processes. This, together with their unique spectroscopic properties that have no parallel in small-molecule copper complexes, has made them the subject of intense study over the last 35 years. This article focuses on three main aspects of type 1 copper proteins: (1) their occurrence, distribution, and classification based on analyses of genomic and expressed sequence tag data; (2) their three-dimensional structures as determined by the well-established tools of single-crystal X-ray diffraction and nuclear magnetic resonance (NMR); and (3) their electronic, spectroscopic, and electron-transfer properties.


  • type 1 copper;
  • blue copper;
  • X-ray crystallography;
  • entatic state;
  • electron paramagnetic resonance;
  • resonance Raman;
  • electron transfer;
  • cupredoxins;
  • phytocyanins