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The proximal hydrogen-bonded residue controls the stability of the compound II intermediate of peroxidases and catalases

AutorRovira, Carme; Fita, Ignacio
Fecha de publicación5-jun-2003
EditorAmerican Chemical Society
CitaciónJournal of Physical Chemistry B 107(22): 5300-5305 (2003)
ResumenThe structural and energetic properties of the compound II intermediate in the catalytic reaction of peroxidases and catalases are compared in order to investigate why catalases, unlike peroxidases, rarely form compound II. Our calculations, based on the density functional theory (DFT)/Car - Parrinello molecular dynamics methodology (CPMD), show that catalase compound II is a stable intermediate with respect to ligand dissociation, with Fe - ligand binding energies comparable to those found for other hemeproteins such as myoglobin and cytochrome c. Nevertheless, catalase shows much weaker iron - ligand bonds compared to those of peroxidase, which is due to the opposite effect of the proximal hydrogen-bonded residues (Arg+ in catalase and Asp- in peroxidase). Comparison with the available structural information suggests that, contrary to the often assumed oxoferryl bond of compound II, some of the reported structures might instead correspond to a hydroxyferryl bond. Some hints on the role of the proximal hydrogen-bonded residues in modulating the stability of the different species during the catalytic reaction are provided.
Versión del editorhttp://dx.doi.org/10.1021/jp0268516
URIhttp://hdl.handle.net/10261/111172
DOI10.1021/jp0268516
Identificadoresdoi: 10.1021/jp0268516
issn: 1520-6106
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