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 26 July 1991:
Vol. 253. no. 5018, pp. 438 - 442
DOI: 10.1126/science.1862344
Prev | Table of Contents | Next

Articles

Science, Vol 253, Issue 5018, 438-442
Copyright © 1991 by American Association for the Advancement of Science

articles

The 2.3 angstrom X-ray structure of nitrite reductase from Achromobacter cycloclastes

JW Godden, S Turley, DC Teller, ET Adman, MY Liu, WJ Payne, and J LeGall

Department of Biochemistry, University of Washington, Seattle 98195.

The three-dimensional crystal structure of the copper-containing nitrite reductase (NIR) from Achromobacter cycloclastes has been determined to 2.3 angstrom (A) resolution by isomorphous replacement. The monomer has two Greek key beta-barrel domains similar to that of plastocyanin and contains two copper sites. The enzyme is a trimer both in the crystal and in solution. The two copper atoms in the monomer comprise one type I copper site (Cu-I; two His, one Cys, and one Met ligands) and one putative type II copper site (Cu-II; three His and one solvent ligands). Although ligated by adjacent amino acids Cu-I and Cu-II are approximately 12.5 A apart. Cu-II is bound with nearly perfect tetrahedral geometry by residues not within a single monomer, but from each of two monomers of the trimer. The Cu-II site is at the bottom of a 12 A deep solvent channel and is the site to which the substrate (NO2-) binds, as evidenced by difference density maps of substrate-soaked and native crystals.


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 »
Electron transfer to nitrite reductase of Rhodobacter sphaeroides 2.4.3: examination of cytochromes c2 and cY..
W. P. Laratta, M. J. Nanaszko, and J. P. Shapleigh (2006)
Microbiology 152, 1479-1488
   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 »
Denitrification Genes Regulate Brucella Virulence in Mice.
S.-H. Baek, G. Rajashekara, G. A. Splitter, and J. P. Shapleigh (2004)
J. Bacteriol. 186, 6025-6031
   Abstract »    Full Text »    PDF »
Side-On Copper-Nitrosyl Coordination by Nitrite Reductase.
E. I. Tocheva, F. I. Rosell, A. G. Mauk, and M. E. P. Murphy (2004)
Science 304, 867-870
   Abstract »    Full Text »    PDF »
Dithionite Reduction Kinetics of the Dissimilatory Copper-containing Nitrite Reductase of Alcalegenes xylosoxidans. THE SO2.- RADICAL BINDS TO THE SUBSTRATE BINDING TYPE 2 COPPER SITE BEFORE THE TYPE 2 COPPER IS REDUCED.
F. K. Yousafzai and R. R. Eady (2002)
J. Biol. Chem. 277, 34067-34073
   Abstract »    Full Text »    PDF »
Characterization of nirV and a gene encoding a novel pseudoazurin in Rhodobacter sphaeroides 2.4.3.
R. Jain and J. P. Shapleigh (2001)
Microbiology 147, 2505-2515
   Abstract »    Full Text »    PDF »
Purification, Characterization, and Genetic Analysis of Cu-Containing Dissimilatory Nitrite Reductase from a Denitrifying Halophilic Archaeon, Haloarcula marismortui.
H. Ichiki, Y. Tanaka, K. Mochizuki, K. Yoshimatsu, T. Sakurai, and T. Fujiwara (2001)
J. Bacteriol. 183, 4149-4156
   Abstract »    Full Text »    PDF »
The Blue Copper-Containing Nitrite Reductase from Alcaligenes xylosoxidans: Cloning of the nirA Gene and Characterization of the Recombinant Enzyme.
M. Prudêncio, R. R. Eady, and G. Sawers (1999)
J. Bacteriol. 181, 2323-2329
   Abstract »    Full Text »
Distinct Roles of Two Heme Centers for Transmembrane Electron Transfer in Cytochrome b561 from Bovine Adrenal Chromaffin Vesicles as Revealed by Pulse Radiolysis.
K. Kobayashi, M. Tsubaki, and S. Tagawa (1998)
J. Biol. Chem. 273, 16038-16042
   Abstract »    Full Text »    PDF »
Structure of Nitrite Bound to Copper-containing Nitrite Reductase from Alcaligenes faecalis. MECHANISTIC IMPLICATIONS.
M. E. P. Murphy, S. Turley, and E. T. Adman (1997)
J. Biol. Chem. 272, 28455-28460
   Abstract »    Full Text »    PDF »
Studies on Protein-Protein Interaction between Copper-containing Nitrite Reductase and Pseudoazurin from Alcaligenes faecalis S-6.
M. Kukimoto, M. Nishiyama, M. Tanokura, E. T. Adman, and S. Horinouchi (1996)
J. Biol. Chem. 271, 13680-13683
   Abstract »    Full Text »    PDF »
The Structure of Copper-nitrite Reductase from Achromobacter cycloclastes at Five pH Values, with NO(2)[IMAGE] Bound and with Type II Copper Depleted.
E. T. Adman, J. W. Godden, and S. Turley (1995)
J. Biol. Chem. 270, 27458-27474
   Abstract »    Full Text »    PDF »
A 110-amino Acid Region within the A1-domain of Coagulation Factor VIII Inhibits Secretion from Mammalian Cells.
K. A. Marquette, D. D. Pittman, and R. J. Kaufman (1995)
J. Biol. Chem. 270, 10297-10303
   Abstract »    Full Text »    PDF »
The Copper-containing Dissimilatory Nitrite Reductase Involved in the Denitrifying System of the Fungus Fusarium oxysporum.
M. Kobayashi and H. Shoun (1995)
J. Biol. Chem. 270, 4146-4151
   Abstract »    Full Text »    PDF »
Electronic structure contributions to function in bioinorganic chemistry.
E. Solomon and M. Lowery (1993)
Science 259, 1575-1581
   Abstract »    PDF »
Crystallographic structure of the nitrogenase iron protein from Azotobacter vinelandii.
M. Georgiadis, H Komiya, P Chakrabarti, D Woo, J. Kornuc, and D. Rees (1992)
Science 257, 1653-1659
   Abstract »    PDF »
Catalytic Roles for Two Water Bridged Residues (Asp-98 and His-255) in the Active Site of Copper-containing Nitrite Reductase.
M. J. Boulanger, M. Kukimoto, M. Nishiyama, S. Horinouchi, and M. E. P. Murphy (2000)
J. Biol. Chem. 275, 23957-23964
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

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