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| [[Image:1ccg.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1ccg| PDB=1ccg | SCENE= }} | | {{STRUCTURE_1ccg| PDB=1ccg | SCENE= }} |
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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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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_7809133}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 7809133 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_7809133}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Mcree, D E.]] | | [[Category: Mcree, D E.]] |
| [[Category: Siegel, H A.]] | | [[Category: Siegel, H A.]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:34:45 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:33:05 2008'' |