Probing the Function of the Tyr-Cys Cross-Link in Metalloenzymes by the Genetic Incorporation of 3-Methylthiotyrosine

Efficient multiple‐electron redox reactions are performed by galactoase oxidase, cysteine dioxygenase, sulfite reductase, and cytochrome c nitrite reductase. A post‐translationally modified tyrosine–cysteine cross‐link (Tyr‐Cys) in their active sites is essential for their functions.

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Bibliographische Detailangaben
Veröffentlicht in:	Angewandte Chemie International Edition 2013-01, Vol.52 (4), p.1203-1207
Hauptverfasser:	Zhou, Qing, Hu, Meirong, Zhang, Wei, Jiang, Li, Perrett, Sarah, Zhou, Juanzuo, Wang, Jiangyun
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Catalytic Domain Crosslinking Cysteine Cysteine - chemistry Cysteine - metabolism Cysteine Dioxygenase - metabolism Cytochromes a1 - chemistry Cytochromes a1 - metabolism Cytochromes c1 - chemistry Cytochromes c1 - metabolism Galactose Oxidase - metabolism Genetics heme proteins metalloenzymes Mutagenesis, Site-Directed Myoglobin - genetics Myoglobin - metabolism Nitrate Reductases - chemistry Nitrate Reductases - metabolism Nitrites non-natural amino acids Oxidase Oxidation-Reduction Redox reactions Reductases Sulfite Reductase (Ferredoxin) - metabolism Sulfites sustainable chemistry tyr-cys cofactor Tyrosine - analogs & derivatives Tyrosine - metabolism Whales
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Beschreibung
Zusammenfassung:	Efficient multiple‐electron redox reactions are performed by galactoase oxidase, cysteine dioxygenase, sulfite reductase, and cytochrome c nitrite reductase. A post‐translationally modified tyrosine–cysteine cross‐link (Tyr‐Cys) in their active sites is essential for their functions.
ISSN:	1433-7851 1521-3773
DOI:	10.1002/anie.201207229