1o7p

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[[Category: oxidoreductase]]
[[Category: oxidoreductase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 15:12:15 2007''
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Revision as of 14:40, 5 November 2007


1o7p, resolution 1.95Å

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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 SO4, FE, EDO, NDH 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.

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

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