Iron oxidation state modulates active site structure in a heme peroxidase.
We have previously shown [Badyal, S. K., et al. (2006) J. Biol. Chem. 281, 24512-24520] that the distal histidine (His42) in the W41A variant of ascorbate peroxidase binds to the heme iron in the ferric form of the protein but that binding of the substrate triggers a conformational change in which H...
المؤلفون الرئيسيون: | Badyal, S, Metcalfe, C, Basran, J, Efimov, I, Moody, P, Raven, E |
---|---|
التنسيق: | Journal article |
اللغة: | English |
منشور في: |
2008
|
مواد مشابهة
-
Evidence for heme oxygenase activity in a heme peroxidase.
حسب: Badyal, S, وآخرون
منشور في: (2009) -
Proton delivery to ferryl heme in a heme peroxidase: enzymatic use of the Grotthuss mechanism.
حسب: Efimov, I, وآخرون
منشور في: (2011) -
Engineering the substrate specificity and reactivity of a heme protein: creation of an ascorbate binding site in cytochrome c peroxidase.
حسب: Murphy, E, وآخرون
منشور في: (2008) -
Heme enzymes. Neutron cryo-crystallography captures the protonation state of ferryl heme in a peroxidase.
حسب: Casadei, C, وآخرون
منشور في: (2014) -
Crystal structure of guaiacol and phenol bound to a heme peroxidase.
حسب: Murphy, E, وآخرون
منشور في: (2012)