Catalytic Mechanism of Pyruvate Formate-Lyase (PFL). A Theoretical Study-Reference-Cited by-同舟云学术

Catalytic Mechanism of Pyruvate Formate-Lyase (PFL). A Theoretical Study

Published:1998-10-22 Issue:44 Volume:120 Page:11449-11455
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Himo Fahmi¹,Eriksson Leif A.¹

Affiliation:

1. Contribution from the Department of Physics, Stockholm University, Box 6730, S-113 85 Stockholm, Sweden

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja9820947

Reference20 articles.

1. For recent reviews see: (a) Knappe, J.; Wagner, A. F. V.MethodsEnzymol.1995,258, 343. (b) Wong, K. K.; Kozarich, J. W. InMetal Ions inBiological Systems; Vol. 30,Metalloenzymes Involving Amino Acid-Residueand Related Radicals; Sigel, H., Sigel A., Eds.; Marcel Dekker: New York, 1994; p 279.

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

3. Hydrogen Exchange of the Glycyl Radical of Pyruvate Formate-Lyase Is Catalyzed by Cysteine 419

4. Pyruvate formate-lyase mechanism involving the protein-based glycyl radical

5. Dioxygen Inactivation of Pyruvate Formate-Lyase: EPR Evidence for the Formation of Protein-Based Sulfinyl and Peroxyl Radicals

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