Spectroscopic characterization of mutations at the Phe41 position in the distal haem pocket of horseradish peroxidase C: structural and functional consequences.

Three mutants of horseradish peroxidase isoenzyme C (HRPC) have been constructed in which the conserved distal aromatic residue Phe(41) has been substituted by Trp, Val or Ala and the properties of the mutant proteins have been compared with that of the wild-type. The ferric and ferrous states have...

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Hlavní autoři: Heering, Hendrik A, Smith, Andrew T, Smulevich, Giulietta
Médium: Artigo
Jazyk:Inglês
Vydáno: 2002
Témata:
Research Article
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC1222510/
https://ncbi.nlm.nih.gov/pubmed/11964158
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