Iron oxidation state modulates active site structure in a heme peroxidase.

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...

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Bibliographic Details
Main Authors:	Badyal, S, Metcalfe, C, Basran, J, Efimov, I, Moody, P, Raven, E
Format:	Journal article
Language:	English
Published:	2008

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