Assembly of 2Fe-2S and 4Fe-4S Clusters in the Anaerobic Ribonucleotide Reductase from Escherichia coli
- 26 June 1999
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 121 (27) , 6344-6350
- https://doi.org/10.1021/ja990073m
Abstract
No abstract availableKeywords
This publication has 18 references indexed in Scilit:
- Activation of the Anaerobic Ribonucleotide Reductase fromEscherichia coliJournal of Biological Chemistry, 1997
- Pyruvate Formate-Lyase Activating Enzyme Is an Iron−Sulfur ProteinJournal of the American Chemical Society, 1997
- Iron-sulfur cluster disassembly in the FNR protein of Escherichia coli by O 2 : [4Fe-4S] to [2Fe-2S] conversion with loss of biological activityProceedings of the National Academy of Sciences, 1997
- The Anaerobic Escherichia coli Ribonucleotide ReductasePublished by Elsevier ,1996
- Site-Directed Mutagenesis and Spectroscopic Characterization of Human Ferrochelatase: Identification of Residues Coordinating the [2Fe-2S] ClusterBiochemistry, 1996
- Formate is the hydrogen donor for the anaerobic ribonucleotide reductase from Escherichia coli.Proceedings of the National Academy of Sciences, 1995
- From RNA to DNA, Why So Many Ribonucleotide Reductases?Science, 1993
- Novel cytotoxic and phytotoxic halogenated sesquiterpenes from the green alga Neomeris annulataJournal of the American Chemical Society, 1989
- Semi-micro methods for analysis of labile sulfide and of labile sulfide plus sulfane sulfur in unusually stable iron-sulfur proteinsAnalytical Biochemistry, 1983
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976