Identification of an Escherichia coli O157:H7 heme oxygenase with tandem functional repeats

DOIResolve DOI: http://doi.org/10.1073/pnas.0504289102
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TypeArticle
Volume102
Issue47
Pages1695516960; # of pages: 6
Subjectanalysis; Bacteria; crystal structure; Escherichia coli; Oxygenases; pha; pharmacology
AbstractHeme oxygenases (HOs) catalyze the oxidation of heme to biliverdin, carbon monoxide (CO), and free iron. Iron acquisition is critical for invading microorganisms to enable survival and growth. Here we report the crystal structure of ChuS, which displays a previously uncharacterized fold and is unique compared with other characterized HOs. Despite only 19% sequence identity between the N- and C-terminal halves, these segments of ChuS represent a structural duplication, with a root-mean-square deviation of 2.1 A between the two repeats. ChuS is capable of using ascorbic acid or cytochrome P450 reductase-NADPH as electron sources for heme oxygenation. CO detection confirmed that ChuS is a HO, and we have identified it in pathogenic Escherichia coli O157:H7. Based on sequence analysis, this HO is present in many bacteria, although not in the E. coli K-12 strain. The N- and C-terminal halves of ChuS are each a functional HO
Publication date
AffiliationNRC Biotechnology Research Institute; National Research Council Canada
Peer reviewedNo
NRC number47495
NPARC number3538864
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Record identifierb8b206ca-3a76-4686-b5bf-691de538cd37
Record created2009-03-01
Record modified2016-05-09
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