Crystal structure of the non-haem iron halogenase SyrB2 in syringomycin biosynthesis
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Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/nature04544.pdf
Reference29 articles.
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2. Hausinger, R. P. Fe(ii)/α-ketoglutarate-dependent hydroxylases and related enzymes. Crit. Rev. Biochem. Mol. Biol. 39, 21–68 (2004)
3. Price, J. C., Barr, E. W., Hoffart, L. M., Krebs, C. & Bollinger, J. M. Jr. Kinetic dissection of the catalytic mechanism of taurine:α-ketoglutarate dioxygenase (TauD) from Escherichia coli. Biochemistry 44, 8138–8147 (2005)
4. Price, J. C., Barr, E. W., Tirupati, B., Bollinger, J. M. Jr & Krebs, C. The first direct characterization of a high-valent iron intermediate in the reaction of an α-ketoglutarate-dependent dioxygenase: a high-spin FeIV complex in taurine/α-ketoglutarate dioxygenase (TauD) from Escherichia coli. Biochemistry 42, 7497–7508 (2003)
5. Vaillancourt, F. H., Yin, J. & Walsh, C. T. SyrB2 in syringomycin E biosynthesis is a non-heme Feii α-ketoglutarate and O2 dependent halogenase. Proc. Natl Acad. Sci. USA 102, 10111–10116 (2005)
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