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The role of T56 in controlling the flexibility of the distal histidine in dehaloperoxidase-hemoglobin from Amphitrite ornata

โœ Scribed by Jiang, Shu; Wright, Iain; Swartz, Paul; Franzen, Stefan


Book ID
122691070
Publisher
Elsevier Science
Year
2013
Tongue
English
Weight
796 KB
Volume
1834
Category
Article
ISSN
1570-9639

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๐Ÿ“œ SIMILAR VOLUMES


Distal histidine conformational flexibil
โœ Chen, Zuxu ;de Serrano, Vesna ;Betts, Laurie ;Franzen, Stefan ๐Ÿ“‚ Article ๐Ÿ“… 2008 ๐Ÿ› International Union of Crystallography ๐ŸŒ English โš– 689 KB

The enzyme dehaloperoxidase (DHP) from the terebellid polychaete Amphitrite ornata is a heme protein which has a globin fold but can function as both a hemoglobin and a peroxidase. As a peroxidase, DHP is capable of converting 2,4,6-trihalophenols to the corresponding 2,6-dihaloquinones in the prese