S K-edge XAS and DFT Calculations on SAM Dependent Pyruvate Formate-Lyase Activating Enzyme: Nature of Interaction between the Fe4S4 Cluster and SAM and its Role in Reactivity-Reference-Cited by-同舟云学术

S K-edge XAS and DFT Calculations on SAM Dependent Pyruvate Formate-Lyase Activating Enzyme: Nature of Interaction between the Fe4S4 Cluster and SAM and its Role in Reactivity

Published:2011-10-28 Issue:46 Volume:133 Page:18656-18662
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Dey Abhishek¹²,Peng Yi³,Broderick William E.³,Hedman Britt⁴,Hodgson Keith O.¹⁴,Broderick Joan B.³,Solomon Edward I.¹⁴

Affiliation:

1. Department of Chemistry, Stanford University, Stanford, California 94305, United States

2. Indian Association for the Cultivation of Science, India, 700032

3. Department of Chemistry and Biochemistry, Montana State University, Bozeman, Montana 59717, United States

4. Stanford Synchrotron Radiation Lightsource, SLAC, Stanford University, Menlo Park, California 94025, United States

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja203780t

Reference48 articles.

1. The Radical SAM Superfamily

2. Biosynthesis of complex iron–sulfur enzymes

3. The [4Fe-4S]1+ Cluster of Pyruvate Formate-Lyase Activating Enzyme Generates the Glycyl Radical on Pyruvate Formate-Lyase: EPR-Detected Single Turnover

4. Post-translational activation introduces a free radical into pyruvate formate-lyase.

5. The free radical in pyruvate formate-lyase is located on glycine-734.

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