Document Detail


A second [2Fe-2S] ferredoxin from Sphingomonas sp. Strain RW1 can function as an electron donor for the dioxin dioxygenase.
MedLine Citation:
PMID:  10735867     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The first step in the degradation of dibenzofuran and dibenzo-p-dioxin by Sphingomonas sp. strain RW1 is carried out by dioxin dioxygenase (DxnA1A2), a ring-dihydroxylating enzyme. An open reading frame (fdx3) that could potentially specify a new ferredoxin has been identified downstream of dxnA1A2, a two-cistron gene (J. Armengaud, B. Happe, and K. N. Timmis, J. Bacteriol. 180:3954-3966, 1998). In the present study, we report a biochemical analysis of Fdx3 produced in Escherichia coli. This third ferredoxin thus far identified in Sphingomonas sp. strain RW1 contained a putidaredoxin-type [2Fe-2S] cluster which was characterized by UV-visible absorption spectrophotometry and electron paramagnetic resonance spectroscopy. The midpoint redox potential of this ferredoxin (E'(0) = -247 +/- 10 mV versus normal hydrogen electrode at pH 8.0) is similar to that exhibited by Fdx1 (-245 mV), a homologous ferredoxin previously characterized in Sphingomonas sp. strain RW1. In in vitro assays, Fdx3 can be reduced by RedA2 (a reductase similar to class I cytochrome P-450 reductases), previously isolated from Sphingomonas sp. strain RW1. RedA2 exhibits a K(m) value of 3.2 +/- 0.3 microM for Fdx3. In vivo coexpression of fdx3 and redA2 with dxnA1A2 confirmed that Fdx3 can serve as an electron donor for the dioxin dioxygenase.
Authors:
J Armengaud; J Gaillard; K N Timmis
Related Documents :
3735307 - One-electron reduction of 2- and 6-methyl-1,4-naphthoquinone bioreductive alkylating ag...
17416687 - Regulation of caffeate respiration in the acetogenic bacterium acetobacterium woodii.
16348557 - Identification of the proton source for the microbial reductive dechlorination of 2,3,4...
18587827 - Reductive dissolution of fe(iii) oxides by pseudomonas sp. 200.
1731927 - Determination of the excited-state lifetimes of the tryptophan residues in barnase, via...
20121177 - Photophysics of squaraine dyes: role of charge-transfer in singlet oxygen production an...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of bacteriology     Volume:  182     ISSN:  0021-9193     ISO Abbreviation:  J. Bacteriol.     Publication Date:  2000 Apr 
Date Detail:
Created Date:  2000-04-18     Completed Date:  2000-04-18     Revised Date:  2013-04-18    
Medline Journal Info:
Nlm Unique ID:  2985120R     Medline TA:  J Bacteriol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  2238-44     Citation Subset:  IM    
Affiliation:
Division of Microbiology, GBF-National Research Center for Biotechnology, D-38124 Braunschweig, Germany. jean.armengaud@ibs.fr
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Electron Spin Resonance Spectroscopy
Electron Transport
Ferredoxins / chemistry,  genetics,  metabolism*
Models, Molecular
Oxygenases / genetics,  metabolism*
Protein Structure, Secondary
Recombinant Proteins / metabolism
Spectrophotometry
Sphingomonas / enzymology*
Chemical
Reg. No./Substance:
0/2Fe-2S ferredoxin; 0/Ferredoxins; 0/Recombinant Proteins; EC 1.13.-/Oxygenases; EC 1.14.99.-/dioxin dioxygenase
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Genetic and biochemical characterization of the pathway in Pantoea citrea leading to pink disease of...
Next Document:  OmpR regulates the stationary-phase acid tolerance response of Salmonella enterica serovar typhimuri...