Title Acinetobacter sp.1의 일산화탄소 산화효소의 특성
Author 조진원 · 김영민 *
Address 연세대학교 이과대학 생물학과
Bibliography Korean Journal of Microbiology, 24(2),133-140, 1986
DOI
Key Words CO dehydrogenase, carbon monoxide, Acinetobacter isolate, carboxydobacteria
Abstract Extracts of CO-autotrophically grown cells of Acinetobacter sp. 1 were shown to use thionin, methylene blue, or 2,6-dichlorophenol-indophenol, but not NAD, NADP, FAD, or FMN, as electron acceptors for the oxidation of CO under strictly anaerobic conditions. The CO dehydrogenase (CO-DH) in the this bacterium was found to be an inducible enzyme. The enzyme activity was determined by an assay based on the CO-dependent reduction of thionin. Maximal reaction rates were found at pH 7.5 and 60℃, and the Arrhenius plot revealed an activation energy of 6.1 kcal/mol(25.5kJ/mol). The K_m for CO was 154uM. Known metalchelating agents tested had no effects on the CO-DH activity. No divalent cations tested affect the enzyme activity significantly except C^2+ which suppressed the activity completely. The enzyme was inhibited by glucose and succinate. The same extracts catalyzed oxidation of hydrogen gas and formate with thionin as electron acceptor. The CO-DH of Acinetobacter sp. 1 was found to have no immunological relationship with that of Pseudomonas carboxydohydrogena.
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