Crystal structure of naphthalene dioxygenase: side-on binding of dioxygen to iron

Science. 2003 Feb 14;299(5609):1039-42. doi: 10.1126/science.1078020.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Binding Sites
  • Catalysis
  • Chemical Phenomena
  • Chemistry, Physical
  • Crystallization
  • Crystallography, X-Ray
  • Dioxygenases
  • Hydroxylation
  • Indoles / metabolism
  • Iron / chemistry
  • Iron / metabolism*
  • Models, Chemical
  • Models, Molecular
  • Molecular Structure
  • Multienzyme Complexes / chemistry*
  • Multienzyme Complexes / metabolism*
  • Naphthalenes
  • Oxidation-Reduction
  • Oxygen / chemistry
  • Oxygen / metabolism*
  • Oxygenases / chemistry*
  • Oxygenases / metabolism*
  • Protein Conformation
  • Protons
  • Pseudomonas / enzymology
  • Stereoisomerism

Substances

  • Indoles
  • Multienzyme Complexes
  • Naphthalenes
  • Protons
  • naphthalene
  • indole
  • Iron
  • Oxygenases
  • Dioxygenases
  • naphthalene dioxygenase
  • Oxygen