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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Identification by ENDOR of Trp191 as the free-radical site in cytochrome c peroxidase compound ES.

The chemical identity of the amino acid free-radical site that represents one of the two oxidizing equivalents stored in the H2O2-oxidized intermediate (compound ES) of the mitochondrial heme enzyme, cytochrome c peroxidase (CcP) has been sought for almost a quarter of a century. Site-directed mutagenesis alone cannot yield this answer. Low-temperature 35-gigahertz (Q-band) electron nuclear double resonance (ENDOR) spectroscopy was used to examine compound ES prepared from proteins containing specifically deuterated methionine or tryptophan, as well as the amino acid replacement Trp51----Phe. The results definitely identify the site of the radical in compound ES as tryptophan, most likely Trp191.[1]

References

  1. Identification by ENDOR of Trp191 as the free-radical site in cytochrome c peroxidase compound ES. Sivaraja, M., Goodin, D.B., Smith, M., Hoffman, B.M. Science (1989) [Pubmed]
 
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