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Related Experiment Videos

NO binding to naphthalene dioxygenase.

Andreas Karlsson1, Juan V Parales, Rebecca E Parales

  • 1Department of Molecular Biology, Biomedical Center, Swedish University of Agricultural Sciences, 75124 Uppsala, Sweden.

Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry
|June 9, 2005
PubMed
Summary

Nitric oxide (NO) binding to naphthalene dioxygenase (NDO) differs from oxygen. While NO binds end-on, oxygen binds side-on, impacting mechanistic studies.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Nitric oxide (NO) is frequently used as a dioxygen (O(2)) analogue in studies of oxygen binding and activation.
  • Naphthalene dioxygenase (NDO) is an enzyme involved in the oxidation of aromatic hydrocarbons.

Purpose of the Study:

  • To determine the crystallographic structure of NDO in complex with nitric oxide (NO).
  • To compare the binding mode of NO to the active site iron with that of O(2).

Main Methods:

  • X-ray crystallography was used to determine the structure of NDO-NO complex.
  • Spectroscopic measurements were performed to analyze NO binding in solution.

Main Results:

  • Crystallographic structures reveal end-on binding of NO to the active-site mononuclear iron of NDO in the presence of indole.

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  • Spectroscopic data correlate with the observed structural binding mode of NO.
  • This end-on binding contrasts with the previously reported side-on binding of O(2) to the NDO active site.

    • Conclusions:

    • While NO shares similarities with O(2), its distinct end-on binding mode to NDO's active site iron has different mechanistic implications.
    • Caution is advised when extrapolating findings from NO studies as direct analogues for O(2) binding mechanisms.