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...
Main Authors: | Gumiero, A, Murphy, E, Metcalfe, C, Moody, P, Raven, E |
---|---|
Formato: | Journal article |
Idioma: | English |
Publicado em: |
2010
|
Registos relacionados
-
Engineering the substrate specificity and reactivity of a heme protein: creation of an ascorbate binding site in cytochrome c peroxidase.
Por: Murphy, E, et al.
Publicado em: (2008) -
Heme enzymes. Neutron cryo-crystallography captures the protonation state of ferryl heme in a peroxidase.
Por: Casadei, C, et al.
Publicado em: (2014) -
Evidence for heme oxygenase activity in a heme peroxidase.
Por: Badyal, S, et al.
Publicado em: (2009) -
Proton delivery to ferryl heme in a heme peroxidase: enzymatic use of the Grotthuss mechanism.
Por: Efimov, I, et al.
Publicado em: (2011) -
Crystal structure of guaiacol and phenol bound to a heme peroxidase.
Por: Murphy, E, et al.
Publicado em: (2012)