Cellular and Molecular Life Sciences CMLS

, Volume 62, Issue 18, pp 2050–2066

Function and molecular evolution of multicopper blue proteins

Review

DOI: 10.1007/s00018-004-5076-x

Cite this article as:
Nakamura, K. & Go, N. Cell. Mol. Life Sci. (2005) 62: 2050. doi:10.1007/s00018-004-5076-x

Abstract.

Multicopper blue proteins (MCBPs) are multidomain proteins that utilize the distinctive redox ability of copper ions. There are a variety of MCBPs that have been roughly classified into three different groups, based on their domain organization and functions: (i) nitrite reductase-type with two domains, (ii) laccase-type with three domains, and (iii) ceruloplasmin-type with six domains. Together, the second and third group are often commonly called multicopper oxidases (MCOs). The rapid accumulation of genome sequence information in recent years has revealed several new types of proteins containing MCBP domains, mainly from bacteria. In this review, the recent research on the functions and structures of MCBPs is summarized, mainly focusing on the new types. The latter half of this review focusses on the twodomain MCBPs, which we propose as the evolutionary intermediate of the MCBP family.

Key words.

Multicopper blue protein (MCBP)multicopper oxidase (MCO)blue-copper-binding site (BCB site)cupredoxinnitrite reductaselaccaseceruloplasminmolecular evolution

Copyright information

© Birkhäuser Verlag, Basel 2005

Authors and Affiliations

  1. 1.Quantum Bioinformatics Group, Center for Promotion of Computational Science and EngineeringJapan Atomic Energy Research InstituteKyotoJapan
  2. 2.Graduate School of Information ScienceNara Institute of Science and TechnologyNaraJapan