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Anke Neumann: Tetrachlorethen-Dehalogenase aus Dehalospirillum multivorans: Isolierung und Charakterisierung des Enzyms sowie Klonierung und Sequenzierung der dafür kodierenden Gene

Anke Neumann

Tetrachlorethen-Dehalogenase aus Dehalospirillum multivorans: Isolierung und Charakterisierung des Enzyms sowie Klonierung und Sequenzierung der dafür kodierenden Gene

Isolation and cloning of tetrachloroethene dehalogenase from Dehalospirillum multivorans

Dehalospirillum multivorans is a strict anaerobe bacterium wich is able to grow on hydrogen and tetrachloroethene as sole energy source. Tetrachloroethene is reductively dechlorinated to cis-1,2-dichloroethene by the tetrachloroethene reductive dehalogenase. This enzyme was studied in crude extracts, purified and characterized. It is a monomer with an app. molecular mass of 57 kDa. One mol dehalogenase contains 1 mol corrinoid and 9.8 mol iron and 8 mol acid labile sulfur. The genes encoding the dehalogenase were cloned and sequenced and non functional expressed in E. coli. An assay for rapid detection of corrinoids was developed based on the reductive dehalogenation of haloaliphatic compounds by Vitamin B12 with reduced methylviologen as electron donor.

  • broschiert: 130 Seiten
    Format: 20,5 x 14,5
    ISBN 978-3-89675-324-3

    40,98 € (Preisbindung aufgehoben)

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