Abstract：
:Chlorite dismutase-like proteins are structurally closely related to functional chlorite dismutases which are heme b-dependent oxidoreductases capable of reducing chlorite to chloride with simultaneous production of dioxygen. Chlorite dismutase-like proteins are incapable of performing this reaction and their biological role is still under discussion. Recently, members of this large protein family were shown to be involved in heme biosynthesis in Gram-positive bacteria, and thus the protein was renamed HemQ in these organisms. In the present work the structural and heme binding properties of the chlorite dismutase-like protein from the Gram-positive pathogen Listeria monocytogenes (LmCld) were analyzed in order to evaluate its potential role as a regulatory heme sensing protein. The homopentameric crystal structure (2.0Å) shows high similarity to chlorite-degrading chlorite dismutases with an important difference in the structure of the putative substrate and heme entrance channel. In solution LmCld is a stable hexamer able to bind the low-spin ligand cyanide. Heme binding is reversible with KD-values determined to be 7.2μM (circular dichroism spectroscopy) and 16.8μM (isothermal titration calorimetry) at pH 7.0. Both acidic and alkaline conditions promote heme release. Presented biochemical and structural data reveal that the chlorite dismutase-like protein from L. monocytogenes could act as a potential regulatory heme sensing and storage protein within heme biosynthesis.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Hofbauer S,Hagmüller A,Schaffner I,Mlynek G,Krutzler M,Stadlmayr G,Pirker KF,Obinger C,Daims H,Djinović-Carugo K,Furtmüller PGdoi
10.1016/j.abb.2015.01.010subject
Has Abstractpub_date
2015-05-15 00:00:00pages
36-48eissn
0003-9861issn
1096-0384pii
S0003-9861(15)00026-0journal_volume
574pub_type
杂志文章abstract：:CopA is a protein formed as part of a copper resistance operon in Pseudomonas syringae pv tomato, but CopA has also been identified from gene library screening as a potential lignin-oxidising enzyme. Few bacterial homologues for bacterial multi-copper laccases have been identified that can assist in lignin degradation...
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更新日期：2009-09-01 00:00:00
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journal_title：Archives of biochemistry and biophysics
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pub_type： 杂志文章
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更新日期：2000-10-15 00:00:00
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journal_title：Archives of biochemistry and biophysics
pub_type： 杂志文章
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更新日期：2014-06-15 00:00:00
