Advertisement
JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Originally published In Press as doi:10.1074/jbc.M111334200 on January 22, 2002

J. Biol. Chem., Vol. 277, Issue 13, 11513-11520, March 29, 2002
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
277/13/11513    most recent
M111334200v1
Right arrow Submit a Letter to Editor
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Haynes, C. A.
Right arrow Articles by Rodgers, D. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Haynes, C. A.
Right arrow Articles by Rodgers, D. W.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Structures of Nitroreductase in Three States
EFFECTS OF INHIBITOR BINDING AND REDUCTION*

Chad A. HaynesDagger , Ronald L. Koder§, Anne-Frances MillerDagger §, and David W. RodgersDagger ||

From the Dagger  Department of Molecular and Cellular Biochemistry and Center for Structural Biology and the § Department of Chemistry, The University of Kentucky, Lexington, Kentucky 40536

The crystal structure of the nitroreductase enzyme from Enterobacter cloacae has been determined for the oxidized form in separate complexes with benzoate and acetate inhibitors and for the two-electron reduced form. Nitroreductase is a member of a group of enzymes that reduce a broad range of nitroaromatic compounds and has potential uses in chemotherapy and bioremediation. The monomers of the nitroreductase dimer adopt an alpha +beta fold and together bind two flavin mononucleotide prosthetic groups at the dimer interface. In the oxidized enzyme, the flavin ring system adopts a strongly bent (16°) conformation, and the bend increases (25°) in the reduced form of the enzyme, roughly the conformation predicted for reduced flavin free in solution. Because free oxidized flavin is planar, the induced bend in the oxidized enzyme may favor reduction, and it may also account for the characteristic inability of the enzyme to stabilize the one electron-reduced semiquinone flavin, which is also planar. Both inhibitors bind over the pyrimidine and central rings of the flavin in partially overlapping sites. Comparison of the two inhibitor complexes shows that a portion of helix H6 can flex to accommodate the differently sized inhibitors suggesting a mechanism for accommodating varied substrates.


* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The atomic coordinates and the structure factors (code 1KQC, 1KQB, 1KQD) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

Present address: The Johnson Foundation, Dept. of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, PA 19104.

|| To whom correspondence should be addressed: Dept. of Molecular and Cellular Biochemistry, The University of Kentucky, 800 Rose St., Lexington, KY 40536. Tel.: 859-257-5205; Fax: 859-323-1037; E-mail: rodgers@focus.gws.uky.edu.


Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
J. Biol. Chem.Home page
S. R. Thomas, P. M. McTamney, J. M. Adler, N. LaRonde-LeBlanc, and S. E. Rokita
Crystal Structure of Iodotyrosine Deiodinase, a Novel Flavoprotein Responsible for Iodide Salvage in Thyroid Glands
J. Biol. Chem., July 17, 2009; 284(29): 19659 - 19667.
[Abstract] [Full Text] [PDF]


Home page
NEJMHome page
J. C. Moreno, W. Klootwijk, H. van Toor, G. Pinto, M. D'Alessandro, A. Leger, D. Goudie, M. Polak, A. Gruters, and T. J. Visser
Mutations in the Iodotyrosine Deiodinase Gene and Hypothyroidism
N. Engl. J. Med., April 24, 2008; 358(17): 1811 - 1818.
[Abstract] [Full Text] [PDF]


Home page
J. Bacteriol.Home page
H. Iwaki, T. Muraki, S. Ishihara, Y. Hasegawa, K. N. Rankin, T. Sulea, J. Boyd, and P. C. K. Lau
Characterization of a Pseudomonad 2-Nitrobenzoate Nitroreductase and Its Catabolic Pathway-Associated 2-Hydroxylaminobenzoate Mutase and a Chemoreceptor Involved in 2-Nitrobenzoate Chemotaxis
J. Bacteriol., May 1, 2007; 189(9): 3502 - 3514.
[Abstract] [Full Text] [PDF]


Home page
MutagenesisHome page
S.G. Salamanca-Pinzon, R. Camacho-Carranza, S.L. Hernandez-Ojeda, and J.J. Espinosa-Aguirre
Nitrocompound activation by cell-free extracts of nitroreductase-proficient Salmonella typhimurium strains
Mutagenesis, November 1, 2006; 21(6): 369 - 374.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
D. van den Hemel, A. Brige, S. N. Savvides, and J. Van Beeumen
Ligand-induced Conformational Changes in the Capping Subdomain of a Bacterial Old Yellow Enzyme Homologue and Conserved Sequence Fingerprints Provide New Insights into Substrate Binding
J. Biol. Chem., September 22, 2006; 281(38): 28152 - 28161.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
K. Ito, M. Nakanishi, W.-C. Lee, H. Sasaki, S. Zenno, K. Saigo, Y. Kitade, and M. Tanokura
Three-dimensional Structure of AzoR from Escherichia coli: AN OXIDEREDUCTASE CONSERVED IN MICROORGANISMS
J. Biol. Chem., July 21, 2006; 281(29): 20567 - 20576.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
P. R. Race, A. L. Lovering, R. M. Green, A. Ossor, S. A. White, P. F. Searle, C. J. Wrighton, and E. I. Hyde
Structural and Mechanistic Studies of Escherichia coli Nitroreductase with the Antibiotic Nitrofurazone: REVERSED BINDING ORIENTATIONS IN DIFFERENT REDOX STATES OF THE ENZYME
J. Biol. Chem., April 8, 2005; 280(14): 13256 - 13264.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2002 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement