An analysis of substrate binding interactions in the heme peroxidase enzymes: a structural perspective.
The interactions of heme peroxidase enzymes with their substrates have been studied for many years, but only in the last decade or so has structural information begun to appear. This review looks at crystal structures for a number of heme peroxidases in complex with a number of (mainly organic) subs...
المؤلفون الرئيسيون: | Gumiero, A, Murphy, E, Metcalfe, C, Moody, P, Raven, E |
---|---|
التنسيق: | Journal article |
اللغة: | English |
منشور في: |
2010
|
مواد مشابهة
-
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) -
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) -
Crystal structure of guaiacol and phenol bound to a heme peroxidase.
حسب: Murphy, E, وآخرون
منشور في: (2012)