Iron-sulfur cluster-containingl-serine dehydratase fromPeptostreptococcus asaccharolyticus: Correlation of the cluster type with enzymatic activity
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(94)00901-5/fullpdf
Reference11 articles.
1. Bacterial l-serine dehydratases: a new family of enzymes containing iron-sulfur clusters
2. Purification and properties of an iron-sulfur-containing and pyridoxal-phosphate-independent l-Serine dehydratase from Peptostreptococcus asaccharolyticus
3. Photoreduction of flavoproteins and other biological compounds catalyzed by deazaflavins. Appendix: photochemical formation of deazaflavin dimers
4. The prosthetic groups in succinate dehydrogenase Number and stoichiometry
5. Three-iron clusters in iron-sulfur proteins
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