Identification of the site of oxidase substrate binding in Scytalidium thermophilum catalase

The catalase from Scytalidium thermophilum is a homotetramer containing a heme d in each active site. Although the enzyme has a classical monofunctional catalase fold, it also possesses oxidase activity towards a number of small organics, including catechol and phenol. In order to further investigat...

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Detalles Bibliográficos
Autores principales: Yuzugullu Karakus, Yonca, Goc, Gunce, Balci, Sinem, Yorke, Briony A., Trinh, Chi H., McPherson, Michael J., Pearson, Arwen R.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2018
Materias:
Research Papers
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6173053/
https://www.ncbi.nlm.nih.gov/pubmed/30289408
http://dx.doi.org/10.1107/S2059798318010628

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6173053/
https://www.ncbi.nlm.nih.gov/pubmed/30289408
http://dx.doi.org/10.1107/S2059798318010628

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