![]()
|
|
||||||||
J. Biol. Chem., Vol. 281, Issue 27, 18660-18667, July 7, 2006
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
From the Department of Chemistry, College of Natural Sciences, Seoul National University, Seoul 151-742, Korea
Nitroalkane compounds are widely used in chemical industry and are also produced by microorganisms and plants. Some nitroalkanes have been demonstrated to be carcinogenic, and enzymatic oxidation of nitroalkanes is of considerable interest. 2-Nitropropane dioxygenases from Neurospora crassa and Williopsis mrakii (Hansenula mrakii), members of one family of the nitroalkane-oxidizing enzymes, contain FMN and FAD, respectively. The enzymatic oxidation of nitroalkanes by 2-nitropropane dioxygenase operates by an oxidase-style catalytic mechanism, which was recently shown to involve the formation of an anionic flavin semiquinone. This represents a unique case in which an anionic flavin semiquinone has been experimentally observed in the catalytic pathway for oxidation catalyzed by a flavin-dependent enzyme. Here we report the first crystal structure of 2-nitropropane dioxygenase from Pseudomonas aeruginosa in two forms: a binary complex with FMN and a ternary complex with both FMN and 2-nitropropane. The structure identifies His152 as the proposed catalytic base, thus providing a structural framework for a better understanding of the catalytic mechanism.
Received for publication, February 22, 2006 , and in revised form, May 1, 2006.
The atomic coordinates and structure factors (code 2GJL and 2GJN) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).
* This work was supported by the Korea Ministry of Science and Technology (Grant NRL-2001). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. S1-S7 and Tables S1 and S2.
1 Recipients of the BK21 fellowship from the Korean Ministry of Education.
2 To whom correspondence should be addressed. Tel.: 82-2-880-6653; Fax: 82-2-889-1568; E-mail: sewonsuh{at}snu.ac.kr.
![]()
CiteULike
Complore
Connotea
Del.icio.us
Digg
Reddit
Technorati What's this?
This article has been cited by other articles:
![]() |
J. Saito, M. Yamada, T. Watanabe, M. Iida, H. Kitagawa, S. Takahata, T. Ozawa, Y. Takeuchi, and F. Ohsawa Crystal structure of enoyl-acyl carrier protein reductase (FabK) from Streptococcus pneumoniae reveals the binding mode of an inhibitor Protein Sci., April 1, 2008; 17(4): 691 - 699. [Abstract] [Full Text] [PDF] |
||||
![]() |
S. Jenni, M. Leibundgut, D. Boehringer, C. Frick, B. Mikolasek, and N. Ban Structure of Fungal Fatty Acid Synthase and Implications for Iterative Substrate Shuttling Science, April 13, 2007; 316(5822): 254 - 261. [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 |