Structural highlights
Function
NDOB_PSEPU Component of the naphthalene dioxygenase (NDO) multicomponent enzyme system which catalyzes the incorporation of both atoms of molecular oxygen into naphthalene to form cis-naphthalene dihydrodiol.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Karlsson A, Parales JV, Parales RE, Gibson DT, Eklund H, Ramaswamy S. Crystal structure of naphthalene dioxygenase: side-on binding of dioxygen to iron. Science. 2003 Feb 14;299(5609):1039-42. PMID:12586937 doi:http://dx.doi.org/10.1126/science.1078020
