1cce
From Proteopedia
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'''CONSTRUCTION OF A BIS-AQUO HEME ENZYME AND REPLACEMENT WITH EXOGENOUS LIGAND''' | '''CONSTRUCTION OF A BIS-AQUO HEME ENZYME AND REPLACEMENT WITH EXOGENOUS LIGAND''' | ||
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[[Category: Siegel, H A.]] | [[Category: Siegel, H A.]] | ||
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Revision as of 09:34, 2 May 2008
CONSTRUCTION OF A BIS-AQUO HEME ENZYME AND REPLACEMENT WITH EXOGENOUS LIGAND
Overview
The crystal structure of the His-175-->Gly (H175G) mutant of cytochrome-c peroxidase (EC 1.11.1.5), missing its only heme ligand, reveals that the histidine is replaced by solvent to give a bisaquo heme protein. This protein retains some residual activity, which can be stimulated or inhibited by addition of exogenous ligands. Structural analysis confirms the binding of imidazole to the heme at the position of the wild-type histidine ligand. This imidazole complex reacts readily with hydrogen peroxide to produce a radical species with novel properties. However, reactivation in this complex is incomplete (approximately 5%), which, in view of the very similar structures of the wild-type and the H175G/imidazole forms, implies a critical role for tethering of the axial ligand in catalysis. This study demonstrates the feasibility of constructing heme enzymes with no covalent link to the protein and with unnatural ligand replacements. Such enzymes may prove useful in studies of electron transfer mechanisms and in the engineering of novel heme-based catalysts.
About this Structure
1CCE is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Construction of a bisaquo heme enzyme and binding by exogenous ligands., McRee DE, Jensen GM, Fitzgerald MM, Siegel HA, Goodin DB, Proc Natl Acad Sci U S A. 1994 Dec 20;91(26):12847-51. PMID:7809133 Page seeded by OCA on Fri May 2 12:34:42 2008
