Related Content
Search Google Scholar for:
|
|
Science 26 July 1991:
Vol. 253. no. 5018, pp. 438 - 442
DOI: 10.1126/science.1862344
|
|
Articles
Science, Vol 253, Issue 5018, 438-442
Copyright © 1991 by American Association for the Advancement of Science
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 »
- Directing the mode of nitrite binding to a copper-containing nitrite reductase from Alcaligenes faecalis S-6: Characterization of an active site isoleucine.
- M. J. Boulanger and M. E.P. Murphy (2003)
Protein Sci.
12, 248-256
| 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 »
|
|
