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Side-on copper-nitrosyl coordination by nitrite reductase.

Elitza I Tocheva1, Federico I Rosell, A Grant Mauk

  • 1Department of Microbiology and Immunology, The University of British Columbia, Vancouver, BC, Canada V6T 1Z3.

Science (New York, N.Y.)
|May 8, 2004
PubMed
Summary

Researchers discovered a novel side-on binding mode for a copper-nitrosyl intermediate in nitrite reductase, crucial for bacterial denitrification. This finding clarifies enzyme catalysis and broadens understanding of nitric oxide interactions in copper proteins.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Structural Biology

Background:

  • Nitrite reductase is key to bacterial denitrification.
  • It catalyzes the reduction of nitrite to nitric oxide.
  • A copper-nitrosyl intermediate is involved in its catalytic cycle.

Purpose of the Study:

  • To elucidate the structure of the copper-nitrosyl intermediate in nitrite reductase.
  • To understand the mechanism of copper-oxygen and copper-nitrogen coordination changes during catalysis.
  • To explore the implications for other copper-containing proteins.

Main Methods:

  • X-ray crystallography was used to determine the structure of the type 2 copper-nitrosyl complex.
  • Comparison with a refined nitrite-bound crystal structure was performed.

Main Results:

  • An unprecedented side-on binding mode of the copper-nitrosyl intermediate was revealed.
  • In this mode, nitrogen and oxygen atoms are nearly equidistant from the copper cofactor.
  • The study explains how coordination shifts between copper-oxygen and copper-nitrogen during catalysis.

Conclusions:

  • The side-on copper-nitrosyl complex represents a novel binding mode in enzyme catalysis.
  • This discovery provides insights into the catalytic mechanism of nitrite reductase.
  • The findings expand the understanding of nitric oxide interactions in copper proteins like superoxide dismutase.