Metalation States versus Enzyme Activities of Cu, Zn-Superoxide Dismutase Probed by Electrospray Ionization Mass Spectrometry-Reference-Cited by-同舟云学术

Metalation States versus Enzyme Activities of Cu, Zn-Superoxide Dismutase Probed by Electrospray Ionization Mass Spectrometry

Published:2008-10-01 Issue:21 Volume:80 Page:8246-8252
ISSN:0003-2700
Container-title:Analytical Chemistry
language:en
Short-container-title:Anal. Chem.

Author:

Yamazaki Yuzo¹,Takao Toshifumi¹

Affiliation:

1. Laboratory of Protein Profiling and Functional Proteomics, Institute for Protein Research, Osaka University, Yamadaoka 3-2, Suita, Osaka 565-0871, Japan

Publisher

American Chemical Society (ACS)

Subject

Analytical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/ac801324b

Reference38 articles.

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3. Crystal structure of bovine Cu,Zn superoxide dismutase at 3 A resolution: chain tracing and metal ligands.

4. Fee, J. A.InSuperoxide and Superoxide Dismutases;Michelson, A. M., McCord, J. M., and Fridovich, I., Eds.Academic Press:London,1977; pp173−192

5. Metal sites of copper proteins. III. Symmetry of copper in bovine superoxide dismutase and its functional significance

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