Abstract:
:We have previously shown that introduction of an engineered Met160 residue in ascorbate peroxidase (S160M variant) leads to the formation of a covalent link between Met160 and the heme vinyl group [Metcalfe, C. L., et al. (2004) J. Am. Chem. Soc. 126, 16242-16248]. In this work, we have used electronic spectroscopy, HPLC, and mass spectrometry to show that the introduction of a tyrosine residue at the same position (S160Y variant) leads, similarly, to the formation of a heme-tyrosine covalent link in an autocatalytic reaction that also leads to formation of a second covalent link from the heme to Trp41 [Pipirou, Z., et al. (2007) Biochemistry 46, 2174-2180]. Stopped-flow and EPR data implicate the involvement of a tyrosyl radical in the reaction mechanism. The results indicate that the heme can support the formation of different types of covalent links under appropriate conditions. The generality of this idea is discussed in the context of other heme enzymes.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Pipirou Z,Bottrill AR,Svistunenko DA,Efimov I,Basran J,Mistry SC,Cooper CE,Raven ELdoi
10.1021/bi7015316subject
Has Abstractpub_date
2007-11-20 00:00:00pages
13269-78issue
46eissn
0006-2960issn
1520-4995journal_volume
46pub_type
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