ArticleJournal of inorganic biochemistry2008
Spectroscopic studies on Arabidopsis ETHE1, a glyoxalase II-like protein.
Article in Journal of inorganic biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 18 citations in OpenAlex.
- Defense responses of sulfur dioxygenase to sulfide stress in the razor clam Sinonovacula constricta.Genes & genomics · 2021Article
- Chemical Biology of HChemical reviews · 2018Review
- Crystal structure of human persulfide dioxygenase: structural basis of ethylmalonic encephalopathy.Human molecular genetics · 2015Article
- The CsoR-like sulfurtransferase repressor (CstR) is a persulfide sensor in Staphylococcus aureus.Molecular microbiology · 2014Article
- Arabidopsis thaliana glyoxalase 2-1 is required during abiotic stress but is not essential under normal plant growth.PloS one · 2014Article
- Characteristics and function of sulfur dioxygenase in Echiuran worm Urechis unicinctus.PloS one · 2013Article
- Altered sulfide (H(2)S) metabolism in ethylmalonic encephalopathy.Cold Spring Harbor perspectives in biology · 2013Review
- Characterization of patient mutations in human persulfide dioxygenase (ETHE1) involved in H2S catabolism.The Journal of biological chemistry · 2012Article
- Arabidopsis ETHE1 encodes a sulfur dioxygenase that is essential for embryo and endosperm development.Plant physiology · 2012Article
- Arabidopsis thaliana mitochondrial glyoxalase 2-1 exhibits beta-lactamase activity.Biochemistry · 2009Article
- Arabidopsis thaliana GLX2-1 contains a dinuclear metal binding site, but is not a glyoxalase 2.The Biochemical journal · 2009Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
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.
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