Unfolding and inactivation of monomeric superoxide dismutase from E. coli by SDS. (Q31957768)

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10 November 2019

title

Unfolding and inactivation of monomeric superoxide dismutase from E. coli by SDS (English)

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10 November 2019

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2

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10 November 2019

Sonia Michaela Melino

4

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10 November 2019

author name string

M Bozzi

1

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10 November 2019

M Sette

3

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10 November 2019

G Rotilio

5

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10 November 2019

M Paci

6

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10 November 2019

publication date

1 August 2001

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International Journal of Biological Macromolecules

10 November 2019

published in

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10 November 2019

volume

29

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10 November 2019

issue

2

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10 November 2019

page(s)

99-105

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Electrostatic recognition between superoxide and copper, zinc superoxide dismutase

10 November 2019

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Conserved Enzyme-Substrate Electrostatic Attraction in Prokaryotic Cu,Zn Superoxide Dismutases

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Evolutionary constraints for dimer formation in prokaryotic Cu,Zn superoxide dismutase

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Unique structural features of the monomeric Cu,Zn superoxide dismutase from Escherichia coli, revealed by X-ray crystallography

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On the Coordination and Oxidation States of the Active-Site Copper Ion in Prokaryotic Cu,Zn Superoxide Dismutases

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Characterization of the spectroscopic properties of the Cu,Co cluster in a prokaryotic superoxide dismutase

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Isolation of an active and heat-stable monomeric form of Cu,Zn superoxide dismutase from the periplasmic space of Escherichia coli

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Role of the dimeric structure in Cu,Zn superoxide dismutase. pH-dependent, reversible denaturation of the monomeric enzyme from Escherichia coli

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Overexpression of a hydrogen peroxide-resistant periplasmic Cu,Zn superoxide dismutase protects Escherichia coli from macrophage killing

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The Cu,Zn superoxide dismutase from Escherichia coli retains monomeric structure at high protein concentration. Evidence for altered subunit interaction in all the bacteriocupreins

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Investigation of the active site of Escherichia coli Cu,Zn superoxide dismutase reveals the absence of the copper-coordinated water molecule. is the water molecule really necessary for the enzymatic mechanism?

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On the quaternary structure of copper-zinc superoxide dismutases. Reversible dissociation into protomers of the isozyme I from wheat germ

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Relationship between functional properties and structure of ovalbumin

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Inactivation and unfolding of aminoacylase during denaturation in sodium dodecyl sulfate solutions

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Unfolding, conformational change of active sites and inactivation of creatine kinase in SDS solutions

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Proton NOE studies on dicopper(II) dicobalt(II) superoxide dismutase

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7 January 2021

Two-dimensional NMR assignment of hyperfine-shifted resonances of very fast relaxing metal binding sites of proteins by NOE spectroscopy. The case of Cu, Co superoxide dismutase

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7 January 2021

A two-dimensional NMR study of bovine Cu, Co superoxide dismutase. Further assignments in the region surrounding the active site

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7 January 2021

NMR evidence for perturbation of the copper coordination sphere upon chemical modification of arginine 141 in bovine Cu,Zn superoxide dismutase

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The crystal structure of the monomeric human SOD mutant F50E/G51E/E133Q at atomic resolution. The enzyme mechanism revisited

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Identifiers

DOI

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10 November 2019

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