{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/71195"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/71195","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Studies on the Methylcoenzyme M Methylreductase System of Methanobacterium Thermoautotrophicum","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.","abstract_html":"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.","abstract_has_math":true,"creators":["Rouviere, Pierre Eugene"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Microbiology","degree_department":null,"school":null,"contributors":["Wolfe, R.S."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2014,"date_issued":"2014-12-16T06:13:05Z","date_published":"2014-12-16T06:13:05Z","updated_at":"2026-07-22T22:26:04Z","subjects":["Biology, Microbiology"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(UMI)AAI8908818"],"render_values":[{"text":"(UMI)AAI8908818","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/71195","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Wolfe, R.S."]},{"key":"dc:creator","label":"Author","values":["Rouviere, Pierre Eugene"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2014-12-16T06:13:05Z","10000-01-01","1988"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Microbiology"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Ph.D."]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["University of Illinois at Urbana-Champaign"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Biology, Microbiology"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["http://hdl.handle.net/2142/71195","(UMI)AAI8908818"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["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.","Made available in DSpace on 2014-12-16T06:13:05Z (GMT). No. of bitstreams: 1 8908818.pdf: 4708185 bytes, checksum: 89d47b7fe43571682688a201631f1031 (MD5) Previous issue date: 1988","Embargo set by: Seth Robbins for item 71361 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","U of I Only","176 p.","Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1988."]},{"key":"dc:title","label":"Title","values":["Studies on the Methylcoenzyme M Methylreductase System of Methanobacterium Thermoautotrophicum"]}]}],"canonical_facts":{"dc:contributor":["Wolfe, R.S."],"dc:creator":["Rouviere, Pierre Eugene"],"dc:date":["2014-12-16T06:13:05Z","10000-01-01","1988"],"dc:description":["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.","Made available in DSpace on 2014-12-16T06:13:05Z (GMT). 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