The [4Fe-4S]1+ Cluster of Pyruvate Formate-Lyase Activating Enzyme Generates the Glycyl Radical on Pyruvate Formate-Lyase: EPR-Detected Single Turnover
- 1 August 2000
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 122 (34) , 8331-8332
- https://doi.org/10.1021/ja002012q
Abstract
No abstract availableThis publication has 21 references indexed in Scilit:
- Pyruvate Formate-Lyase-Activating Enzyme: Strictly Anaerobic Isolation Yields Active Enzyme Containing a [3Fe–4S]+ ClusterBiochemical and Biophysical Research Communications, 2000
- Spectroscopic Evidence for the Participation of an Allylic Analogue of the 5‘-Deoxyadenosyl Radical in the Reaction of Lysine 2,3-AminomutaseJournal of the American Chemical Society, 1999
- Assembly of 2Fe-2S and 4Fe-4S Clusters in the Anaerobic Ribonucleotide Reductase from Escherichia coliJournal of the American Chemical Society, 1999
- Lipoic Acid Biosynthesis: LipA Is an Iron−Sulfur ProteinJournal of the American Chemical Society, 1999
- S-Adenosylmethionine-Dependent Reduction of Lysine 2,3-Aminomutase and Observation of the Catalytically Functional Iron−Sulfur Centers by Electron Paramagnetic ResonanceBiochemistry, 1998
- [2Fe-2S] to [4Fe-4S] Cluster Conversion in Escherichia coli Biotin SynthaseBiochemistry, 1997
- Pyruvate Formate-Lyase Activating Enzyme Is an Iron−Sulfur ProteinJournal of the American Chemical Society, 1997
- Biotin Synthase: Purification, Characterization as a [2Fe-2S]Cluster Protein, and in vitro Activity of the Escherichia coli bioB Gene ProductBiochemistry, 1994
- Characterization of iron-sulfur clusters in lysine 2,3-aminomutase by electron paramagnetic resonance spectroscopyBiochemistry, 1992
- Importance of organic radicals in enzymic cleavage of unactivated carbon-hydrogen bondsChemical Reviews, 1990