{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/71182"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/71182","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Component C of the Methylcoenzyme M Methylreductase","abstract":"U of I Only","abstract_html":"U of I Only","abstract_has_math":false,"creators":["Hartzell, Patricia Louise"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Microbiology","degree_department":null,"school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2014,"date_issued":"2014-12-16T06:12:59Z","date_published":"2014-12-16T06:12:59Z","updated_at":"2026-07-22T22:26:04Z","subjects":["Chemistry, Biochemistry"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(UMI)AAI8711807"],"render_values":[{"text":"(UMI)AAI8711807","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/71182","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:creator","label":"Author","values":["Hartzell, Patricia Louise"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2014-12-16T06:12:59Z","10000-01-01","1987"]},{"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":["Chemistry, Biochemistry"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["http://hdl.handle.net/2142/71182","(UMI)AAI8711807"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["U of I Only","Component C, an enzyme in the methylcoenzyme M methylreductase complex of methanogens, has been proposed to contain the catalytic site for methyl group reduction from CH(,3)-S-CH(,2)CH(,2)SO(,3)('-) (methylcoenzyme M). Component C, a hexamer in an (alpha)(,2), (beta)(,2), (gamma)(,2) configuration, contains a chromophore F(,430), coenzyme M and component B (7-mercaptoheptanoylthreonine phosphate). There are two mol of F(,430), a unique nickel tetrapyrrole, per mol of component C. Coenzyme M, the C-1 carrier in the terminal step of methanogenesis, is also present in a ratio of two mol per mol of protein.","The role of the nickel tetrapyrrole, F(,430), in catalysis was tested by isolating and purifying F(,430) and each of the subunits of component C. Recovery of maximal enzyme activity required each subunit, F(,430), and coenzyme M. When F(,430) was omitted from the reassociation mixture, the M(,r) 300,000 apoprotein was formed, but was unable to function in the methanogenic assay. Isomers of the nickel tetrapyrrole differed in their ability to reassociate with the enzyme subunits and yielded holoenzyme with altered specific activities. Salt extracted F(,430), a six-coordinate form, gave optimal reassociation and specific activity whereas the four-coordinate heat extracted F(,430) reassociated poorly with the enzyme subunits.","The function of the bound C-1 carrier, coenzyme M, in the enzyme was examined with radiolabel tracing during in vitro methanogenesis using a double labeled substrate, C('3)H(,3)-S-CH(,2)CH(,2)('35)SO(,3)('-). The bound form of the coenzyme was found to be HS-CH(,2)CH(,2)SO(,3)('-) and the stoichiometry of 2 mol of HS-CoM per mol of enzyme was confirmed. The incorporation was slow and was not stoichiometric with methane production during catalysis. The incorporation was specific for the thioethanesulfonate moiety of CH(,3)-S-CoM; labeled HS-CoM was not incorporated into the enzyme during methanogenesis.","The substrate analogue, bromoethanesulfonate (BES), was found to competitively inhibit methanogenesis from methylcoenzyme M. The target of inhibition was component C.","Made available in DSpace on 2014-12-16T06:12:59Z (GMT). No. of bitstreams: 1 8711807.pdf: 6490546 bytes, checksum: 5ff6d7a041e89aa23b64497275672309 (MD5) Previous issue date: 1987","Embargo set by: Seth Robbins for item 71348 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","226 p.","Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1987."]},{"key":"dc:title","label":"Title","values":["Component C of the Methylcoenzyme M Methylreductase"]}]}],"canonical_facts":{"dc:creator":["Hartzell, Patricia Louise"],"dc:date":["2014-12-16T06:12:59Z","10000-01-01","1987"],"dc:description":["U of I Only","Component C, an enzyme in the methylcoenzyme M methylreductase complex of methanogens, has been proposed to contain the catalytic site for methyl group reduction from CH(,3)-S-CH(,2)CH(,2)SO(,3)('-) (methylcoenzyme M). Component C, a hexamer in an (alpha)(,2), (beta)(,2), (gamma)(,2) configuration, contains a chromophore F(,430), coenzyme M and component B (7-mercaptoheptanoylthreonine phosphate). There are two mol of F(,430), a unique nickel tetrapyrrole, per mol of component C. Coenzyme M, the C-1 carrier in the terminal step of methanogenesis, is also present in a ratio of two mol per mol of protein.","The role of the nickel tetrapyrrole, F(,430), in catalysis was tested by isolating and purifying F(,430) and each of the subunits of component C. Recovery of maximal enzyme activity required each subunit, F(,430), and coenzyme M. When F(,430) was omitted from the reassociation mixture, the M(,r) 300,000 apoprotein was formed, but was unable to function in the methanogenic assay. Isomers of the nickel tetrapyrrole differed in their ability to reassociate with the enzyme subunits and yielded holoenzyme with altered specific activities. Salt extracted F(,430), a six-coordinate form, gave optimal reassociation and specific activity whereas the four-coordinate heat extracted F(,430) reassociated poorly with the enzyme subunits.","The function of the bound C-1 carrier, coenzyme M, in the enzyme was examined with radiolabel tracing during in vitro methanogenesis using a double labeled substrate, C('3)H(,3)-S-CH(,2)CH(,2)('35)SO(,3)('-). The bound form of the coenzyme was found to be HS-CH(,2)CH(,2)SO(,3)('-) and the stoichiometry of 2 mol of HS-CoM per mol of enzyme was confirmed. The incorporation was slow and was not stoichiometric with methane production during catalysis. The incorporation was specific for the thioethanesulfonate moiety of CH(,3)-S-CoM; labeled HS-CoM was not incorporated into the enzyme during methanogenesis.","The substrate analogue, bromoethanesulfonate (BES), was found to competitively inhibit methanogenesis from methylcoenzyme M. The target of inhibition was component C.","Made available in DSpace on 2014-12-16T06:12:59Z (GMT). No. of bitstreams: 1 8711807.pdf: 6490546 bytes, checksum: 5ff6d7a041e89aa23b64497275672309 (MD5) Previous issue date: 1987","Embargo set by: Seth Robbins for item 71348 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","226 p.","Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1987."],"dc:identifier":["http://hdl.handle.net/2142/71182","(UMI)AAI8711807"],"dc:subject":["Chemistry, Biochemistry"],"dc:title":["Component C of the Methylcoenzyme M Methylreductase"],"dc:type":["text"],"thesis:degree_discipline":["Microbiology"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Ph.D."],"thesis:institution_name":["University of Illinois at Urbana-Champaign"]},"updated_at":"2026-07-22T22:26:04Z"}