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|Title:||Studies on the Methylcoenzyme M Methylreductase System of Methanobacterium Thermoautotrophicum|
|Author(s):||Rouviere, Pierre Eugene|
|Doctoral Committee Chair(s):||Wolfe, R.S.|
|Department / Program:||Microbiology|
|Degree Granting Institution:||University of Illinois at Urbana-Champaign|
|Abstract:||The methylcoenzyme M methylreductase system of Methanobacterium thermoautotrophicum catalyzes the reductive demethylation of methylcoenzyme M by H$\sb2$. It had been previously shown to consist of four protein fractions, named components A1, A2, A3, and C. In this work, component A2 was purified to homogeneity using ATP-agarose affinity chromatography. This suggested that component A2 was involved in the activation of the system by ATP. The utilization of the dialdehyde of ATP showed that component A3 was also involved in this activation. When various sources of electrons were used, it was shown that the methylreductase system had two separate requirements for reducing equivalents, one of them to reactivate the methylreductase and the other to reduce methylcoenzyme M. Component A3 was then resolved in two fractions. One of them, called A4, contained one of the hydrogenases of Methanobacterium. The other, called component A3 per se, consisted of an FeS protein with a molecular weight of 500,000. A model for the functioning of the methylcoenzyme M methylreductase system, including components A1, A2, A3, A4, and C, as well as the dual requirement for reducing equivalents, was presented.
A simple technique using denaturing polyacrylamide gel electrophoresis of component C to study the taxonomy of methanogenic bacteria was also presented.
Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1988.
|Date Available in IDEALS:||2014-12-16|