1o7p
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Binding of oxygen to iron is exploited in several biological and chemical | + | Binding of oxygen to iron is exploited in several biological and chemical processes. Although computational and spectroscopic results have suggested side-on binding, only end-on binding of oxygen to iron has been observed in crystal structures. We have determined structures of naphthalene dioxygenase that show a molecular oxygen species bound to the mononuclear iron in a side-on fashion. In a complex with substrate and dioxygen, the dioxygen molecule is lined up for an attack on the double bond of the aromatic substrate. The structures reported here provide the basis for a reaction mechanism and for the high stereospecificity of the reaction catalyzed by naphthalene dioxygenase. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Pseudomonas putida]] | [[Category: Pseudomonas putida]] | ||
[[Category: Eklund, H.]] | [[Category: Eklund, H.]] | ||
| - | [[Category: Gibson, D | + | [[Category: Gibson, D T.]] |
[[Category: Karlsson, A.]] | [[Category: Karlsson, A.]] | ||
| - | [[Category: Parales, J | + | [[Category: Parales, J V.]] |
| - | [[Category: Parales, R | + | [[Category: Parales, R E.]] |
[[Category: Ramaswamy, S.]] | [[Category: Ramaswamy, S.]] | ||
[[Category: EDO]] | [[Category: EDO]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''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 14:14:24 2008'' |
Revision as of 12:14, 21 February 2008
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NAPHTHALENE 1,2-DIOXYGENASE, PRODUCT COMPLEX
Overview
Binding of oxygen to iron is exploited in several biological and chemical processes. Although computational and spectroscopic results have suggested side-on binding, only end-on binding of oxygen to iron has been observed in crystal structures. We have determined structures of naphthalene dioxygenase that show a molecular oxygen species bound to the mononuclear iron in a side-on fashion. In a complex with substrate and dioxygen, the dioxygen molecule is lined up for an attack on the double bond of the aromatic substrate. The structures reported here provide the basis for a reaction mechanism and for the high stereospecificity of the reaction catalyzed by naphthalene dioxygenase.
About this Structure
1O7P is a Protein complex structure of sequences from Pseudomonas putida with , , , and as ligands. Active as Naphthalene 1,2-dioxygenase, with EC number 1.14.12.12 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Crystal structure of naphthalene dioxygenase: side-on binding of dioxygen to iron., Karlsson A, Parales JV, Parales RE, Gibson DT, Eklund H, Ramaswamy S, Science. 2003 Feb 14;299(5609):1039-42. PMID:12586937
Page seeded by OCA on Thu Feb 21 14:14:24 2008
Categories: Naphthalene 1,2-dioxygenase | Protein complex | Pseudomonas putida | Eklund, H. | Gibson, D T. | Karlsson, A. | Parales, J V. | Parales, R E. | Ramaswamy, S. | EDO | FE | FES | NDH | SO4 | Aromatic hydrocarbon catabolism oxidoreductase | Enzyme-substrate complex | Iron-sulfur | Non-heme iron dioxygenase | Oxidoreductase
