2d6c
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The incorporation of an artificially created metal complex into an | + | The incorporation of an artificially created metal complex into an apomyoglobin is one of the attractive methods in a series of hemoprotein modifications. Single crystals of sperm whale myoglobin reconstituted with 13,16-dicarboxyethyl-2,7-diethyl-3,6,12,17-tetramethylporphycenatoiron(III ) were obtained in the imidazole buffer, and the 3D structure with a 2.25-A resolution indicates that the iron porphycene, a structural isomer of hemin, is located in the normal position of the heme pocket. Furthermore, it was found that the reconstituted myoglobin catalyzed the H2O2-dependent oxidations of substrates such as guaiacol, thioanisole, and styrene. At pH 7.0 and 20 degrees C, the initial rate of the guaiacol oxidation is 11-fold faster than that observed for the native myoglobin. Moreover, the stopped-flow analysis of the reaction of the reconstituted protein with H2O2 suggested the formation of two reaction intermediates, compounds II- and III-like species, in the absence of a substrate. It is a rare example that compound III is formed via compound II in myoglobin chemistry. The enhancement of the peroxidase activity and the formation of the stable compound III in myoglobin with iron porphycene mainly arise from the strong coordination of the Fe-His93 bond. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Matsuo, T.]] | [[Category: Matsuo, T.]] | ||
[[Category: Murata, D.]] | [[Category: Murata, D.]] | ||
| - | [[Category: RSGI, RIKEN | + | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] |
[[Category: Sato, H.]] | [[Category: Sato, H.]] | ||
[[Category: Shiro, Y.]] | [[Category: Shiro, Y.]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:55:52 2008'' |
Revision as of 14:55, 21 February 2008
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Crystal structure of myoglobin reconstituted with iron porphycene
Overview
The incorporation of an artificially created metal complex into an apomyoglobin is one of the attractive methods in a series of hemoprotein modifications. Single crystals of sperm whale myoglobin reconstituted with 13,16-dicarboxyethyl-2,7-diethyl-3,6,12,17-tetramethylporphycenatoiron(III ) were obtained in the imidazole buffer, and the 3D structure with a 2.25-A resolution indicates that the iron porphycene, a structural isomer of hemin, is located in the normal position of the heme pocket. Furthermore, it was found that the reconstituted myoglobin catalyzed the H2O2-dependent oxidations of substrates such as guaiacol, thioanisole, and styrene. At pH 7.0 and 20 degrees C, the initial rate of the guaiacol oxidation is 11-fold faster than that observed for the native myoglobin. Moreover, the stopped-flow analysis of the reaction of the reconstituted protein with H2O2 suggested the formation of two reaction intermediates, compounds II- and III-like species, in the absence of a substrate. It is a rare example that compound III is formed via compound II in myoglobin chemistry. The enhancement of the peroxidase activity and the formation of the stable compound III in myoglobin with iron porphycene mainly arise from the strong coordination of the Fe-His93 bond.
About this Structure
2D6C is a Single protein structure of sequence from Physeter catodon with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure and peroxidase activity of myoglobin reconstituted with iron porphycene., Hayashi T, Murata D, Makino M, Sugimoto H, Matsuo T, Sato H, Shiro Y, Hisaeda Y, Inorg Chem. 2006 Dec 25;45(26):10530-6. PMID:17173408
Page seeded by OCA on Thu Feb 21 16:55:52 2008
Categories: Physeter catodon | Single protein | Hayashi, T. | Hisaeda, Y. | Makino, M. | Matsuo, T. | Murata, D. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Sato, H. | Shiro, Y. | Sugimoto, H. | HME | IMD | Hemoprotein | Myoglobin | Oxygen storage/transport | Porphycene | Riken structural genomics/proteomics initiative | Rsgi | Structural genomics
