Document Type

Article

Language

eng

Publication Date

9-2008

Publisher

Elsevier

Source Publication

Journal of Inorganic Biochemistry

Source ISSN

0162-0134

Original Item ID

DOI: 10.1016/j.jinorgbio.2008.06.003

Abstract

ETHE1 (ethylmalonic encephalopathy protein 1) is a β-lactamase fold-containing protein that is essential for the survival of a range of organisms. In spite of the apparent importance of this enzyme, very little is known about its function or biochemical properties. In this study Arabidopsis ETHE1 was over-expressed and purified and shown to bind tightly to 1.2 ± 0.2 equivalents of iron. 1H NMR and EPR studies demonstrate that the predominant oxidation state of Fe in ETHE1 is Fe(II), and NMR studies confirm that two histidines are bound to Fe(II). EPR studies show that there is no antiferromagnetically coupled Fe(III)Fe(II) center in ETHE1. Gel filtration studies reveal that ETHE1 is a dimer in solution, which is consistent with previous crystallographic studies. Although very similar in terms of amino acid sequence to glyoxalase II, ETHE1 exhibits no thioester hydrolase activity, and activity screening assays reveal that ETHE1 exhibits low level esterase activity. Taken together, ETHE1 is a novel, mononuclear Fe(II)-containing member of the β-lactamase fold superfamily.

Comments

Accepted version. Journal of Inorganic Biochemistry, Vol. 102, No. 9 (September 2008): 1825-1830. DOI. © 2008 Elsevier. Used with permission.

NOTICE: this is the author’s version of a work that was accepted for publication in Journal of Inorganic Biochemistry. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Journal of Inorganic Biochemistry, VOL 102, ISSUE 9, September 2008, DOI.

Brian Bennett was affiliated with Medical College of Wisconsin at the time of publication.

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