Electron-Nuclear Double Resonance Spectroscopic Evidence That S-Adenosylmethionine Binds in Contact with the Catalytically Active [4Fe−4S]+ Cluster of Pyruvate Formate-Lyase Activating Enzyme-Reference-Cited by-同舟云学术

Electron-Nuclear Double Resonance Spectroscopic Evidence That S-Adenosylmethionine Binds in Contact with the Catalytically Active [4Fe−4S]+ Cluster of Pyruvate Formate-Lyase Activating Enzyme

Published:2002-03-01 Issue:12 Volume:124 Page:3143-3151
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Walsby Charles J.¹,Hong Wei¹,Broderick William E.¹,Cheek Jennifer¹,Ortillo Danilo¹,Broderick Joan B.¹,Hoffman Brian M.¹

Affiliation:

1. Contribution from the Department of Chemistry, Northwestern University, Evanston, Illinois 60208-3113, and Department of Chemistry, Michigan State University, East Lansing, Michigan 48824-1322

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja012034s

Reference57 articles.

1. Iron-Sulfur Clusters: Nature's Modular, Multipurpose Structures

2. Adenosylmethionine-dependent iron-sulfur enzymes: versatile clusters in a radical new role

3. Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods

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