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Methyltetrahydrofolate:corrinoid/iron-sulfur Protein Methyltransferase (MeTr): Protonation State of the Ligand and Active-Site Residues

Alonso, Hernan; Cummins, Peter; Gready, Jill

Description

Methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase (MeTr) catalyzes the transfer of the N5-methyl group from N5- methyltetrahydrofolate (CH3THF) to the cobalt center of a corrinoid/iron-sulfur protein, a reaction similar to that of cobalamin-dependent methionine synthase (MetH). For such a reaction to occur, CH3THF is expected to be activated by a stereospecific protonation at the N5 position. It has been shown experimentally that binding to MeTr is associated with a pK a...[Show more]

CollectionsANU Research Publications
Date published: 2009
Type: Journal article
URI: http://hdl.handle.net/1885/38619
Source: Journal of Physical Chemistry B
DOI: 10.1021/jp900181g

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