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Published on: October 23, 2016
Properties of stable hydrogenase from the purple sulfur bacterium Lamprobacter modestohalophilus
O A Zadvorny1, N A Zorin, I N Gogotov
1Institute of Basic Biological Problems, Russian Academy of Sciences, Pushchino 142290, Moscow Region, Russia. olegz@issp.serpukhov.su
Abstract:
Some properties of a hydrogenase from the recently isolated phototrophic sulfur bacterium Lamprobacter modestohalophilus strain Syvash and its resistance to a number of inactivating factors have been investigated. The enzyme consists of two subunits, 64 and 30 kD; pI = 4.5. The optimal pH was 8.5-9.5 for hydrogen uptake and 4.0 for H2 evolution. Hydrogenase preparations were resistant to the effects of O2, CO, and temperature, revealing high stability under storage. A considerable inactivation of the enzyme was observed at temperatures above 80 degrees C; the temperature optimum of methyl viologen reduction by H2 was 85 degrees C. Inhibitory effects of Ni2+, Cd2+, and Mg2+ on the hydrogenase activity were shown to be reversible and competitive with respect to methyl viologen in the hydrogen oxidation reaction.
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