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Arch Biochem Biophys. 2012 Sep 15;525(2):102-10. doi: 10.1016/j.abb.2011.12.011. Epub 2011 Dec 23.

Thirty years of heme catalases structural biology.

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1
Institut de Biologia Molecular de Barcelona (CSIC) and IRB Barcelona, Parc Científic de Barcelona, Baldiri i Reixac 10-12, 08028-Barcelona, Spain.

Abstract

About thirty years ago the crystal structures of the heme catalases from Penicillium vitale (PVC) and, a few months later, from bovine liver (BLC) were published. Both enzymes were compact tetrameric molecules with subunits that, despite their size differences and the large phylogenetic separation between the two organisms, presented a striking structural similarity for about 460 residues. The high conservation, confirmed in all the subsequent structures determined, suggested a strong pressure to preserve a functional catalase fold, which is almost exclusively found in these mono-functional heme catalases. However, even in the absence of the catalase fold an efficient catalase activity is also found in the heme containing catalase-peroxidase proteins. The structure of these broad substrate range enzymes, reported for the first time less than ten years ago from the halophilic archaebacterium Haloarcula marismortui (HmCPx) and from the bacterium Burkholderia pseudomallei (BpKatG), showed a heme pocket closely related to that of plant peroxidases, though with a number of unique modifications that enable the catalase reaction. Despite the wealth of structural information already available, for both monofunctional catalases and catalase-peroxidases, a number of unanswered major questions require continuing structural research with truly innovative approaches.

PMID:
22209752
DOI:
10.1016/j.abb.2011.12.011
[Indexed for MEDLINE]
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