Novel types of two-domain multi-copper oxidases: Possible missing links in the evolution

Kensuke Nakamura; Takeshi Kawabata; Kei Yura; Nobuhiro Go

doi:10.1016/S0014-5793(03)01000-7

Novel types of two-domain multi-copper oxidases: Possible missing links in the evolution

Kensuke Nakamura^*, Takeshi Kawabata, Kei Yura, Nobuhiro Go

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

55 Citations (Scopus)

Abstract

An analysis of the genome sequence database revealed novel types of two-domain multi-copper oxidases. The two-domain proteins have the conspicuous combination of blue-copper and inter-domain trinuclear copper binding residues, which is common in ceruloplasmin and ascorbate oxidase but not in nitrite reductase, and therefore are considered to retain the characteristics of the plausible ancestral form of ceruloplasmin and ascorbate oxidase. A possible evolutionary relationship of these proteins is proposed.

Original language	English
Pages (from-to)	239-244
Number of pages	6
Journal	FEBS Letters
Volume	553
Issue number	3
DOIs	https://doi.org/10.1016/S0014-5793(03)01000-7
Publication status	Published - 2003 Oct 23
Externally published	Yes

Keywords

Copper binding protein
Cupredoxin
Cyanobacterium
Genome sequence
Phylogeny
Rhizobium

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/S0014-5793(03)01000-7

Cite this

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title = "Novel types of two-domain multi-copper oxidases: Possible missing links in the evolution",

abstract = "An analysis of the genome sequence database revealed novel types of two-domain multi-copper oxidases. The two-domain proteins have the conspicuous combination of blue-copper and inter-domain trinuclear copper binding residues, which is common in ceruloplasmin and ascorbate oxidase but not in nitrite reductase, and therefore are considered to retain the characteristics of the plausible ancestral form of ceruloplasmin and ascorbate oxidase. A possible evolutionary relationship of these proteins is proposed.",

keywords = "Copper binding protein, Cupredoxin, Cyanobacterium, Genome sequence, Phylogeny, Rhizobium",

author = "Kensuke Nakamura and Takeshi Kawabata and Kei Yura and Nobuhiro Go",

note = "Funding Information: We thank Dr. Gautam Basu for helpful discussions. Our research was supported by the Special Coordination Funds Promoting Science and Technology, and a Grant-in-Aid for Scientific Research on Priority Areas (C) {\textquoteleft}Genome Information Science{\textquoteright} from the Ministry of Education, Culture, Sports, Science and Technology (MEXT), Japan.",

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T1 - Novel types of two-domain multi-copper oxidases

T2 - Possible missing links in the evolution

AU - Nakamura, Kensuke

AU - Kawabata, Takeshi

AU - Yura, Kei

AU - Go, Nobuhiro

N1 - Funding Information: We thank Dr. Gautam Basu for helpful discussions. Our research was supported by the Special Coordination Funds Promoting Science and Technology, and a Grant-in-Aid for Scientific Research on Priority Areas (C) ‘Genome Information Science’ from the Ministry of Education, Culture, Sports, Science and Technology (MEXT), Japan.

PY - 2003/10/23

Y1 - 2003/10/23

N2 - An analysis of the genome sequence database revealed novel types of two-domain multi-copper oxidases. The two-domain proteins have the conspicuous combination of blue-copper and inter-domain trinuclear copper binding residues, which is common in ceruloplasmin and ascorbate oxidase but not in nitrite reductase, and therefore are considered to retain the characteristics of the plausible ancestral form of ceruloplasmin and ascorbate oxidase. A possible evolutionary relationship of these proteins is proposed.

AB - An analysis of the genome sequence database revealed novel types of two-domain multi-copper oxidases. The two-domain proteins have the conspicuous combination of blue-copper and inter-domain trinuclear copper binding residues, which is common in ceruloplasmin and ascorbate oxidase but not in nitrite reductase, and therefore are considered to retain the characteristics of the plausible ancestral form of ceruloplasmin and ascorbate oxidase. A possible evolutionary relationship of these proteins is proposed.

KW - Copper binding protein

KW - Cupredoxin

KW - Cyanobacterium

KW - Genome sequence

KW - Phylogeny

KW - Rhizobium

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JO - FEBS Letters

JF - FEBS Letters

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Novel types of two-domain multi-copper oxidases: Possible missing links in the evolution

Abstract

Keywords

ASJC Scopus subject areas

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