Synthesis of redox-active fluorinated 5-hydroxytryptophans as molecular reporters for biological electron transfer. Issue 25 (24th February 2021)

• Record Type: Journal Article
• Authors: Ohler, Amanda; Long, Hanna; Ohgo, Kei; Tyson, Kristin; Murray, David; Davis, Amanda; Whittington, Chris; Hvastkovs, Eli G.; Duffy, Liam; Haddy, Alice; Sargent, Andrew L.; Allen, William E.; Offenbacher, Adam R.
• Is Part Of: Chemical communications. Volume 57:Issue 25(2021)
• Page Start: 3107
• Page End: 3110
• Publication Date: 2021-02-24
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1039/d1cc00187f
• Languages: English
• ISSNs: 1359-7345

Abstract

Abstract : Chemoenzymatic synthesis of fluorinated 5-hydroxytryptophans provides a novel set of non-canonical tryptophan amino acids useful for probes of biological electron transfer reactions. Abstract : Fluorinated 5-hydroxytryptophans (F n -5HOWs) were synthesized in gram scale quantities and incorporated into a β-hairpin peptide and the protein azurin. The redox-active F n -5HOWs exhibit unique radical spectroscopic signatures that expand the function of ; 5HOW as probes for biological electron transfer.