Good and bad of Cu/Zn-superoxide dismutase controlled by metal ions and disulfide bonds

Yoshiaki Furukawa

doi:10.1246/CL.200770

Good and bad of Cu/Zn-superoxide dismutase controlled by metal ions and disulfide bonds

Yoshiaki Furukawa

Department of Chemistry

Research output: Contribution to journal › Review article › peer-review

Abstract

Cu/Zn-superoxide dismutase (SOD1) is a metalloenzyme that catalyzes the disproportionation of superoxide. This review summarizes intracellular processes for metal binding and disulfide formation in SOD1, both of which are essential to stabilization of the protein structure as well as its enzymatic function. Also, failure of those processes as a possible cause of a neurodegenerative disease through protein misfolding will be described.

Original language	English
Pages (from-to)	331-341
Number of pages	11
Journal	Chemistry Letters
Volume	50
Issue number	2
DOIs	https://doi.org/10.1246/CL.200770
Publication status	Published - 2021

Keywords

Metalloprotein
Neurodegenerative disease
Protein folding

ASJC Scopus subject areas

Chemistry(all)

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10.1246/CL.200770

Cite this

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title = "Good and bad of Cu/Zn-superoxide dismutase controlled by metal ions and disulfide bonds",

abstract = "Cu/Zn-superoxide dismutase (SOD1) is a metalloenzyme that catalyzes the disproportionation of superoxide. This review summarizes intracellular processes for metal binding and disulfide formation in SOD1, both of which are essential to stabilization of the protein structure as well as its enzymatic function. Also, failure of those processes as a possible cause of a neurodegenerative disease through protein misfolding will be described.",

keywords = "Metalloprotein, Neurodegenerative disease, Protein folding",

author = "Yoshiaki Furukawa",

note = "Funding Information: This work was supported by Grants-in-Aid 19H05765 for Scientific Research on Innovative Areas from the Ministry of Education, Culture, Sports, Science and Technology of Japan and also supported by Grants-in-Aid for Programs for the Advancement of Research in Core Projects under Keio University{\textquoteright}s Longevity Initiative and for the Advancement of Next Generation Research Projects from Keio University. Publisher Copyright: {\textcopyright} 2021 The Chemical Society of Japan.",

year = "2021",

doi = "10.1246/CL.200770",

language = "English",

volume = "50",

pages = "331--341",

journal = "Chemistry Letters",

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publisher = "Chemical Society of Japan",

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TY - JOUR

T1 - Good and bad of Cu/Zn-superoxide dismutase controlled by metal ions and disulfide bonds

AU - Furukawa, Yoshiaki

N1 - Funding Information: This work was supported by Grants-in-Aid 19H05765 for Scientific Research on Innovative Areas from the Ministry of Education, Culture, Sports, Science and Technology of Japan and also supported by Grants-in-Aid for Programs for the Advancement of Research in Core Projects under Keio University’s Longevity Initiative and for the Advancement of Next Generation Research Projects from Keio University. Publisher Copyright: © 2021 The Chemical Society of Japan.

PY - 2021

Y1 - 2021

N2 - Cu/Zn-superoxide dismutase (SOD1) is a metalloenzyme that catalyzes the disproportionation of superoxide. This review summarizes intracellular processes for metal binding and disulfide formation in SOD1, both of which are essential to stabilization of the protein structure as well as its enzymatic function. Also, failure of those processes as a possible cause of a neurodegenerative disease through protein misfolding will be described.

AB - Cu/Zn-superoxide dismutase (SOD1) is a metalloenzyme that catalyzes the disproportionation of superoxide. This review summarizes intracellular processes for metal binding and disulfide formation in SOD1, both of which are essential to stabilization of the protein structure as well as its enzymatic function. Also, failure of those processes as a possible cause of a neurodegenerative disease through protein misfolding will be described.

KW - Metalloprotein

KW - Neurodegenerative disease

KW - Protein folding

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DO - 10.1246/CL.200770

M3 - Review article

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SN - 0366-7022

VL - 50

SP - 331

EP - 341

JO - Chemistry Letters

JF - Chemistry Letters

IS - 2

ER -

Good and bad of Cu/Zn-superoxide dismutase controlled by metal ions and disulfide bonds

Abstract

Keywords

ASJC Scopus subject areas

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