Rubredoxin reductase from Alcanivorax borkumensis: Expression and characterization

Authors

  • Afsaneh Teimoori,

    1. Dept. of Biochemistry, Institute of Biochemistry and Biophysics (IBB), University of Tehran, Tehran, Iran
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  • Shahin Ahmadian,

    1. Dept. of Biochemistry, Institute of Biochemistry and Biophysics (IBB), University of Tehran, Tehran, Iran
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  • Armin Madadkar-Sobhani,

    1. Dept. of Biochemistry, Institute of Biochemistry and Biophysics (IBB), University of Tehran, Tehran, Iran
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  • Bijan Bambai

    Corresponding author
    1. Dept. of Industrial and Environmental Biotechnology, Division of Industrial Microbiology, National Institute for Genetic Engineering and Biotechnology (NIGEB), Tehran, Iran
    2. Dept. of Biology, Faculty of Biological Sciences, Shahid Beheshti University, GC, Tehran 19839, Iran
    • Dept. of Industrial and Environmental Biotechnology, Division of Industrial Microbiology, National Institute for Genetic Engineering and Biotechnology (NIGEB), Tehran, Iran
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Abstract

Oil pollution is an environmental problem of increasing importance. Alcanivoraxborkumensis, with a high potential for biotechnological applications, is a key marine hydrocarbonoclastic bacterium and plays a critical role in the bioremediation of oil-polluted marine systems. In oil degrading bacteria, the first step of alkane degradation is catalyzed by a monooxygenase. The reducing electrons are tunneled from NAD(P)H via rubredoxin, one of the most primitive metalloproteins, to the hydroxylase. Rubredoxin reductase is a flavoprotein catalyzing the reduction of rubredoxin. There are two rubredoxin genes, alkG and rubA, in A. borkumensis genome. In this work, the genes encoding rubredoxin reductase (ABO_0162, rubB) and AlkG(ABO_2708, alkG) were cloned and functionally overexpressed in E. coli. Our results demonstrate that RubB could reduce AlkG, therefore compensating for the absence of AlkT, also a rubredoxin reductase, missing in A. borkumensis SK2 genome. These results will increase our knowledge concerning biological alkane degradation and will lead us to design more efficient biotransformation and bioremediation systems. © 2011 American Institute of Chemical Engineers Biotechnol. Prog., 2011

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