Proton delivery to ferryl heme in a heme peroxidase: enzymatic use of the Grotthuss mechanism.
We test the hypothesized pathway by which protons are passed from the substrate, ascorbate, to the ferryl oxygen in the heme enzyme ascorbate peroxidase (APX). The role of amino acid side chains and bound solvent is demonstrated. We investigated solvent kinetic isotope effects (SKIE) for the wild-ty...
Main Authors: | Efimov, I, Badyal, S, Metcalfe, C, Macdonald, I, Gumiero, A, Raven, E, Moody, P |
---|---|
Format: | Journal article |
Language: | English |
Published: |
2011
|
Similar Items
-
Heme enzymes. Neutron cryo-crystallography captures the protonation state of ferryl heme in a peroxidase.
by: Casadei, C, et al.
Published: (2014) -
Nature of the ferryl heme in compounds I and II.
by: Gumiero, A, et al.
Published: (2011) -
Evidence for heme oxygenase activity in a heme peroxidase.
by: Badyal, S, et al.
Published: (2009) -
Iron oxidation state modulates active site structure in a heme peroxidase.
by: Badyal, S, et al.
Published: (2008) -
An analysis of substrate binding interactions in the heme peroxidase enzymes: a structural perspective.
by: Gumiero, A, et al.
Published: (2010)