1o7h: Difference between revisions
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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 14:14:15 2008'' | ||
Revision as of 15:14, 21 February 2008
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NAPHTHALENE 1,2-DIOXYGENASE WITH OXIDIZED RIESKE IRON SULPHUR CENTER SITE.
OverviewOverview
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 StructureAbout this Structure
1O7H 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.
ReferenceReference
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
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