Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 7 May 2004:
Vol. 304. no. 5672, pp. 867 - 870
DOI: 10.1126/science.1095109
Prev | Table of Contents | Next

Reports

Side-On Copper-Nitrosyl Coordination by Nitrite Reductase

Elitza I. Tocheva,1 Federico I. Rosell,2 A. Grant Mauk,2 Michael E. P. Murphy1,2*

A copper-nitrosyl intermediate forms during the catalytic cycle of nitrite reductase, the enzyme that mediates the committed step in bacterial denitrification. The crystal structure of a type 2 copper-nitrosyl complex of nitrite reductase reveals an unprecedented side-on binding mode in which the nitrogen and oxygen atoms are nearly equidistant from the copper cofactor. Comparison of this structure with a refined nitrite-bound crystal structure explains how coordination can change between copper-oxygen and copper-nitrogen during catalysis. The side-on copper-nitrosyl in nitrite reductase expands the possibilities for nitric oxide interactions in copper proteins such as superoxide dismutase and prions.

1 Department of Microbiology and Immunology, The University of British Columbia, Vancouver, BC, Canada V6T 1Z3.
2 Department of Biochemistry and Molecular Biology, The University of British Columbia, Vancouver, BC, Canada V6T 1Z3.

* To whom correspondence should be addressed. E-mail: memurphy{at}interchange.ubc.ca

Read the Full Text


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
pH Dependence of Copper Geometry, Reduction Potential, and Nitrite Affinity in Nitrite Reductase.
F. Jacobson, A. Pistorius, D. Farkas, W. De Grip, O. Hansson, L. Sjolin, and R. Neutze (2007)
J. Biol. Chem. 282, 6347-6355
   Abstract »    Full Text »    PDF »
A Random-sequential Mechanism for Nitrite Binding and Active Site Reduction in Copper-containing Nitrite Reductase.
H. J. Wijma, L. J. C. Jeuken, M. P. Verbeet, F. A. Armstrong, and G. W. Canters (2006)
J. Biol. Chem. 281, 16340-16346
   Abstract »    Full Text »    PDF »
Atomic resolution structures of resting-state, substrate- and product-complexed Cu-nitrite reductase provide insight into catalytic mechanism.
S. V. Antonyuk, R. W. Strange, G. Sawers, R. R. Eady, and S. S. Hasnain (2005)
PNAS 102, 12041-12046
   Abstract »    Full Text »    PDF »


ADVERTISEMENT
Click Me!

ADVERTISEMENT
Click Me!

To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)