DNA and RNA enzymes with peroxidase activity — An investigation into the mechanism of action

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2006
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Abstract
A DNA–hemin complex (PS2.M–hemin), and its RNA counterpart (rPS2.M–hemin), have previously been reported, in the presence of nitrogenous buffers such as HEPES, to show enhanced peroxidative activity relative to both uncomplexed hemin and a control DNA–hemin complex (Chem. Biol. 5, 505, 1998). A kinetic analysis of these two hemin-utilizing nucleic acid enzymes provides key insights into the mechanisms for their catalyzed peroxidation reactions. First, control experiments indicate that charge on the added detergent, required for solubility reasons, has little effect on the efficiency of the nucleic-acid-catalyzed reactions. Second, the key functional impact of the two nucleic acid frameworks, either DNA or RNA, appears to be a reduction in the acidity of a water molecule coordinated to the iron atom of the hemin that is bound to the ribozyme and DNAzyme scaffolds. This effect could result from a polar environment and possibly hydrogen bond(s) at the axial position of the hemin, along with favourable hydrophobic interactions for the periphery of the porphyrin ring. Third, the basic component of the buffer enhances the activities; this likely results from a general-base-catalyzed process. Cumulatively, these data supply important clues as to how biopolymers other than a protein can complex with hemin to form productive peroxidase enzymes.Key words: ribozyme, DNAzyme, hemin, peroxidase, mechanism, guanine quadruplex.
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Authors Paola Travascio,Dipankar Sen,Andrew J Bennet;Paola Travascio;Dipankar Sen;Andrew J Bennet;
Journal canadian journal of chemistry
Year 2006
DOI
10.1139/v06-057
URL
https://sciprofiles.com/publication/view/818678209ffa76cca02156a8affa611c
Keywords
protein peroxidase functional dnazyme hydrophobic hemin buffers ribozyme nitrogenous nucleic

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