Characterization of Enzymes of the Methylcoenzyme M Reductase System From Methanobacterium Thermoautotrophicum and Identification of a Factor Required for Growth of Methanomicrobium Mobile

The reduction of 2-(methylthio) ethanesulfonate (CH$\sb3$-S-coenzyme M, CH$\sb3$-S-CoM) by methanogenic archaea is catalyzed by a methylcoenzyme M reductase (MR). In Methanobacterium thermoautotrophicum strain $\Delta$H, this reaction has been shown to require minimally two additional protein components (A2 and A3a), as well as ATP and a second reductant. Although component A2 has been purified to homogeneity, proteins comprising component A3a have only been partially resolved, and the functions of these components remain unknown.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Microbiology

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2014

Author dc:creator

• Kuhner, Carla Heidi

Contributors dc:contributor

• Wolfe, R.S.

• Biology, Microbiology

Identifier

(UMI)AAI9411677

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/72526