Subunit dissociation and metal binding by Escherichia coli apo-manganese superoxide dismutase-Reference-Cited by-同舟云学术

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Subunit dissociation and metal binding by Escherichia coli apo-manganese superoxide dismutase

Published:2011-01 Issue:2 Volume:505 Page:213-225
ISSN:0003-9861
Container-title:Archives of Biochemistry and Biophysics
language:en
Short-container-title:Archives of Biochemistry and Biophysics

Author:

Whittaker Mei M.,Lerch Thomas F.,Kirillova Olga,Chapman Michael S.,Whittaker James W.

Funder

National Institutes of Health

American Heart Association

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics

Reference42 articles.

1. SUPEROXIDE RADICAL AND SUPEROXIDE DISMUTASES

2. Determination and analysis of the 2 Å structure of copper, zinc superoxide dismutase

3. Structure-function in Escherichia coli iron superoxide dismutase: Comparisons with the manganese enzyme from Thermus thermophilus

4. Crystal structure of Escherichia coli manganese superoxide dismutase at 2.1-Å resolution

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1. Identifying Metal Binding Sites in Proteins Using Homologous Structures, the MADE Approach;Journal of Chemical Information and Modeling;2023-08-09

2. Characterization of ancestral Fe/Mn superoxide dismutases indicates their cambialistic origin;Protein Science;2022-09-21

3. Semiholoenzyme optimizes activity and stability of a hyperthermostable iron-superoxide dismutase;Biochemical and Biophysical Research Communications;2019-10

4. A Single Outer-Sphere Mutation Stabilizes apo-Mn Superoxide Dismutase by 35 °C and Disfavors Mn Binding;Biochemistry;2017-07-13

5. Iron incorporation into MnSOD A (bacterial Mn-dependent superoxide dismutase) leads to the formation of a peroxidase/catalase implicated in oxidative damage to bacteria;Biochimica et Biophysica Acta (BBA) - General Subjects;2015-09

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