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Biomolecular Concepts

Editor-in-Chief: Di Cera, Enrico


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1868-503X
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Volume 1, Issue 1

Issues

Structure and molecular evolution of multicopper blue proteins

Hirofumi Komori
  • Department of Life Science, Graduate School of Life Science, University of Hyogo, 3-2-1 Koto, Kamigori-cho, Ako-gun, Hyogo 678-1297, Japan
  • RIKEN SPring-8 Center, 1-1-1 Koto, Mikazuki-cho, Sayo-gun, Hyogo 679-5248, Japan
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Yoshiki Higuchi
  • Department of Life Science, Graduate School of Life Science, University of Hyogo, 3-2-1 Koto, Kamigori-cho, Ako-gun, Hyogo 678-1297, Japan
  • RIKEN SPring-8 Center, 1-1-1 Koto, Mikazuki-cho, Sayo-gun, Hyogo 679-5248, Japan
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2010-03-16 | DOI: https://doi.org/10.1515/bmc.2010.004

Abstract

The multicopper blue protein family, which contains cupredoxin-like domains as a structural unit, is one of the most diverse groups of proteins. This protein family is divided into two functionally different types of enzymes: multicopper oxidase and nitrite reductase. Multicopper oxidase catalyzes the oxidation of the substrate and then reduces dioxygen. The structures of many multicopper oxidases are already known, and until recently they were classified into two main groups: the three- and six-domain types. Both function as monomers and have three spectroscopically different copper sites: Types I (blue), II, and III (tri-nuclear). Nitrite reductase is a closely related protein that contains Types I and II (mono-nuclear) coppers but reduces nitrite instead of dioxygen. Nitrite reductase, which consists of two domains, forms a homotrimer. Multicopper oxidase and nitrite reductase share similar structural architectures and also contain Type I copper. Therefore, it is proposed that they have a common ancestor protein. Recently, some two-domain type multicopper oxidases have been found and their crystal structures have been determined. They have a trimeric quaternary structure and contain an active site at the molecular interface such as nitrite reductase. These results support previous hypotheses and provide an insight into the molecular evolution of multicopper blue proteins.

Keywords: ascorbate reductase; blue copper; ceruloplasmin; laccase; multicopper oxidase; nitrite reductase; Type I copper

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Published Online: 2010-03-16

Published in Print: 2010-05-01


Citation Information: BioMolecular Concepts, Volume 1, Issue 1, Pages 31–40, ISSN (Online) 1868-503X, ISSN (Print) 1868-5021, DOI: https://doi.org/10.1515/bmc.2010.004.

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[1]
Hirofumi Komori, Kunishige Kataoka, Sakiko Tanaka, Nana Matsuda, Yoshiki Higuchi, and Takeshi Sakurai
Acta Crystallographica Section F Structural Biology Communications, 2016, Volume 72, Number 7, Page 558
[2]
Hirofumi Komori and Yoshiki Higuchi
Journal of Biochemistry, 2015, Volume 158, Number 4, Page 293
[3]
K. A. Moshkov, V. N. Zaitsev, T. V. Grishina, and V. E. Stefanov
Journal of Evolutionary Biochemistry and Physiology, 2014, Volume 50, Number 3, Page 189
[4]
Hirofumi Komori, Ryosuke Sugiyama, Kunishige Kataoka, Kentaro Miyazaki, Yoshiki Higuchi, and Takeshi Sakurai
Acta Crystallographica Section D Biological Crystallography, 2014, Volume 70, Number 3, Page 772

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