Reconstitution of Cu,Zn-superoxide dismutase by the Cu(I).glutathione complex.

Ciriolo, Maria Rosa; Desideri, Alessandro; Paci, Maurizio; Rotilio, Giuseppe

doi:10.1016/s0021-9258(19)38552-7

Cited by 146 publications

(29 citation statements)

References 27 publications

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“…The activation of Sod1 proteins without Pro at these positions in ccs1⌬ yeast cells (12,28) or in ccs1 Ϫ/Ϫ null mice suggests that the copper ion may be provided by labile Cu(I) complexes in the yeast cytosol (e.g. Cu-glutathione) (30,31). These results also highlight the link between copper acquisition and disulfide bond formation.…”

mentioning

confidence: 82%

Copper-zinc superoxide dismutase is activated through a sulfenic acid intermediate at a copper ion entry site

Fetherolf

Boyd

Taylor

et al. 2017

Journal of Biological Chemistry

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Metallochaperones are a diverse family of trafficking molecules that provide metal ions to protein targets for use as cofactors. The copper chaperone for superoxide dismutase (Ccs1) activates immature copper-zinc superoxide dismutase (Sod1) by delivering copper and facilitating the oxidation of the Sod1 intramolecular disulfide bond. Here, we present structural, spectroscopic, and cell-based data supporting a novel copper-induced mechanism for Sod1 activation. Ccs1 binding exposes an electropositive cavity and proposed "entry site" for copper ion delivery on immature Sod1. Copper-mediated sulfenylation leads to a sulfenic acid intermediate that eventually resolves to form the Sod1 disulfide bond with concomitant release of copper into the Sod1 active site. Sod1 is the predominant disulfide bond-requiring enzyme in the cytoplasm, and this copper-induced mechanism of disulfide bond formation obviates the need for a thiol/disulfide oxidoreductase in that compartment.

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mentioning

confidence: 82%

Copper-zinc superoxide dismutase is activated through a sulfenic acid intermediate at a copper ion entry site

Fetherolf

Boyd

Taylor

et al. 2017

Journal of Biological Chemistry

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“…Glutathione can not only reduce Cu(II) to Cu(I), but also bind strongly to soft metals, such as Cu(I), by forming very stable complexes even in the presence of oxygen. 7,35 Glutathione is the most abundant intracellular nonprotein thiol and is present in all living cells in concentrations varying from 1 to 6 mM. Therefore, complex of Cu(I) to glutathione (GSH-Cu(I)) may provide a pooling mechanism for Cu(I) in living cells.…”

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confidence: 99%

Visual and quantitative detection of copper ions using magnetic silica nanoparticles clicked on multiwalled carbon nanotubes

Song¹,

Qu²,

Xu³

et al. 2010

Chem. Commun.

128

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“…Increased levels of GSH were observed in hepatoma cells treated with copper and inhibition of GSH synthesis with buthionine sulfoximine reduced the incorporation of copper into metallothioneins (Freedman and Peisach 1989b). It was also shown in vitro that Cu + -GSH could mediate Cu + -transfer into metal depleted metallothionein or copper-free Cu,Zn-superoxide dismutase (Ascone et al 1993;Ciriolo et al 1990;Ferreira et al 1993). In vivo pulse-chase experiments with radioactive Cu + revealed that Cu + could also be transferred in the reverse direction from metallothionein to GSH and then to Cu,Zn-superoxide dismutase (Freedman and Peisach 1989a).…”

Section: The State Of Cytoplasmic Coppermentioning

confidence: 99%

How Bacteria Handle Copper

Magnani

Solioz

Microbiology Monographs

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Copper in biological systems presents a formidable problem: it is essential for life, yet highly reactive and a potential source of cell damage. Tight control of copper is thus a cellular necessity. To meet this challenge, cells have evolved pumps for transmembranous transport, chaperones for intracellular routing, oxidases and reductases to change the oxidation state of copper, and regulators to control gene expression in response to copper. These systems are complemented by specific mechanisms for the insertion of copper into enzymes. Copper homeostasis has evolved early in evolution and some components have been conserved from bacteria to humans. This has allowed researchers to apply knowledge across phyla and even involving human copper homeostatic diseases to elucidate the fundamental mechanism of cellular copper homeostasis. After an introduction to the properties of copper and its role in biological systems, some of the best studied bacterial systems for copper homeostasis will be discussed.

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Reconstitution of Cu,Zn-superoxide dismutase by the Cu(I).glutathione complex.

Cited by 146 publications

References 27 publications

Copper-zinc superoxide dismutase is activated through a sulfenic acid intermediate at a copper ion entry site

Copper-zinc superoxide dismutase is activated through a sulfenic acid intermediate at a copper ion entry site

Visual and quantitative detection of copper ions using magnetic silica nanoparticles clicked on multiwalled carbon nanotubes

How Bacteria Handle Copper

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