Tuning the formation of a covalent haem-protein link by selection of reductive or oxidative conditions as exemplified by ascorbate peroxidase.
Previous work [Metcalfe, Ott, Patel, Singh, Mistry, Goff and Raven (2004) J. Am. Chem. Soc. 126, 16242-16248] has shown that the introduction of a methionine residue (S160M variant) close to the 2-vinyl group of the haem in ascorbate peroxidase leads to the formation of a covalent haem-methionine li...
Main Authors: | Metcalfe, C, Daltrop, O, Ferguson, S, Raven, E |
---|---|
פורמט: | Journal article |
שפה: | English |
יצא לאור: |
2007
|
פריטים דומים
-
Autocatalytic formation of a covalent link between tryptophan 41 and the heme in ascorbate peroxidase.
מאת: Pipirou, Z, et al.
יצא לאור: (2007) -
Autocatalytic formation of green heme: evidence for H2O2-dependent formation of a covalent methionine-heme linkage in ascorbate peroxidase.
מאת: Metcalfe, C, et al.
יצא לאור: (2004) -
Peroxide-dependent formation of a covalent link between Trp51 and the heme in cytochrome c peroxidase.
מאת: Pipirou, Z, et al.
יצא לאור: (2009) -
Triazine probes targeting ascorbate peroxidases in plants
מאת: Morimoto, K, et al.
יצא לאור: (2019) -
Engineering the substrate specificity and reactivity of a heme protein: creation of an ascorbate binding site in cytochrome c peroxidase.
מאת: Murphy, E, et al.
יצא לאור: (2008)