A Single Outer-Sphere Mutation Stabilizes apo-Mn Superoxide Dismutase by 35 °C and Disfavors Mn Binding-Reference-Cited by-同舟云学术

A Single Outer-Sphere Mutation Stabilizes apo-Mn Superoxide Dismutase by 35 °C and Disfavors Mn Binding

Published:2017-07-13 Issue:29 Volume:56 Page:3787-3799
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Miller Anne-Frances¹²^ORCID,Wang Ting¹

Affiliation:

1. Department of Chemistry, University of Kentucky, 505 Rose Street, Lexington, Kentucky 40506-0055, United States

2. Department of Molecular and Cellular Biochemistry and Center for Structural Biology, University of Kentucky, 741 South Limestone Street, Lexington, Kentucky 40536-0509, United States

Funder

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.7b00175

Reference69 articles.

1. Superoxide Dismutases and Superoxide Reductases

2. Manganese and iron superoxide dismutases are structural homologs.

3. Superoxide dismutases: Ancient enzymes and new insights

4. A comparison of evolutionary rates of the two major kinds of superoxide dismutase

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