Radical formation on a conserved tyrosine residue is crucial for DyP activity. | Arch Biochem Biophys;537(2): 161-7, 2013 Sep 15. | MEDLINE

Main content 1 Search 2 Footer 3

+A A -A High contrast

VHL Regional Portal

Information and Knowledge for Health

Advanced Search EVID@Easy

Radical formation on a conserved tyrosine residue is crucial for DyP activity.

Strittmatter, Eric; Wachter, Sabrina; Liers, Christiane; Ullrich, René; Hofrichter, Martin; Plattner, Dietmar A; Piontek, Klaus.

Affiliation

Strittmatter E; Institute of Organic Chemistry, Albert-Ludwigs-University, Albertstrasse 21, 79104 Freiburg, Germany.

Arch Biochem Biophys ; 537(2): 161-7, 2013 Sep 15.

Article in En | MEDLINE | ID: mdl-23876237

Subject(s)
Key words

Catalysis; Dye-decolorizing peroxidases (DyPs); Enzyme assay; Heme; Mass spectrometry; PROLI/NO; Spin trapping; Tryptophan; Tyrosine

Search on Google

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Peroxidases / Tyrosine / Anthraquinones / Coloring Agents Language: En Journal: Arch Biochem Biophys Year: 2013 Document type: Article Affiliation country: Alemania

Search on Google

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Peroxidases / Tyrosine / Anthraquinones / Coloring Agents Language: En Journal: Arch Biochem Biophys Year: 2013 Document type: Article Affiliation country: Alemania