1o7n: Difference between revisions

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[[Category: oxidoreductase]]
[[Category: oxidoreductase]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:04:28 2007''
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:45:35 2007''

Revision as of 16:40, 30 October 2007

File:1o7n.gif


1o7n, resolution 1.40Å

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NAPHTHALENE 1,2-DIOXYGENASE, TERNARY COMPLEX WITH DIOXYGEN AND INDOLE

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

1O7N is a [Protein complex] structure of sequences from [Pseudomonas putida] with SO4, FE, EDO, IND, OXY and FES as [ligands]. Active as [Naphthalene 1,2-dioxygenase], with EC number [1.14.12.12]. Structure known Active Site: AC1. 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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OCA