Faculty Collaboration Database

Spectroscopic studies on Arabidopsis ETHE1, a glyoxalase II-like protein. J Inorg Biochem 2008 Sep;102(9):1825-30

Date

07/29/2008

Pubmed ID

18656261

Pubmed Central ID

PMC2556177

DOI

10.1016/j.jinorgbio.2008.06.003

Scopus ID

2-s2.0-48849106057 (requires institutional sign-in at Scopus site)   17 Citations

Abstract

ETHE1 (ethylmalonic encephalopathy protein 1) is a beta-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. (1)H 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 beta-lactamase fold superfamily.

Author List

Holdorf MM, Bennett B, Crowder MW, Makaroff CA

Author

Brian Bennett D.Phil. Professor and Chair in the Physics department at Marquette University

MESH terms used to index this publication - Major topics in bold

Arabidopsis
Arabidopsis Proteins
Dimerization
Electron Spin Resonance Spectroscopy
Ferrous Compounds
Iron
Magnetic Resonance Spectroscopy
Manganese
Oxidation-Reduction
Protein Binding
Thiolester Hydrolases
Zinc