{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/70537"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/70537","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Characterization of a Bromoperoxidase From the Marine Algae Penicillus Capitatus","abstract":"The soluble emzyme bromperoxidase isolated from the marine green algae P. capitatus is capable of catalyzing halide oxiations while in the presence of peroxide. Protein purification and characterization of this enzyme showed that the prosthetic group is ferric protoporphyrin IX and that the enzyme consists of two equal molecular weight subunits whose combined weight is approximately 100,000. Bromoperoxidase contains no detectable level of carbohydrate.","abstract_html":"The soluble emzyme bromperoxidase isolated from the marine green algae P. capitatus is capable of catalyzing halide oxiations while in the presence of peroxide. Protein purification and characterization of this enzyme showed that the prosthetic group is ferric protoporphyrin IX and that the enzyme consists of two equal molecular weight subunits whose combined weight is approximately 100,000. Bromoperoxidase contains no detectable level of carbohydrate.","abstract_has_math":false,"creators":["Manthey, John Anthony"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Biochemistry","degree_department":null,"school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2014,"date_issued":"2014-12-15T23:43:49Z","date_published":"2014-12-15T23:43:49Z","updated_at":"2026-07-22T22:26:03Z","subjects":["Biophysics, General"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(UMI)AAI8502234"],"render_values":[{"text":"(UMI)AAI8502234","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/70537","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:creator","label":"Author","values":["Manthey, John Anthony"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2014-12-15T23:43:49Z","10000-01-01","1984"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biochemistry"]},{"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":["Biophysics, General"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["http://hdl.handle.net/2142/70537","(UMI)AAI8502234"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["The soluble emzyme bromperoxidase isolated from the marine green algae P. capitatus is capable of catalyzing halide oxiations while in the presence of peroxide. Protein purification and characterization of this enzyme showed that the prosthetic group is ferric protoporphyrin IX and that the enzyme consists of two equal molecular weight subunits whose combined weight is approximately 100,000. Bromoperoxidase contains no detectable level of carbohydrate.","Initial characterization of the oxidized intermediates of bromoperoxidase which result from the protein's reaction with peroxide molecules shows that bromoperoxidase forms typical Compound I and Compound II species. Electron para-magnetic resonance (EPR) measurements failed to show any radical signal associated with Compound I. A third oxidized intermediate, termed Compound III forms as a result of the reaction of peroxide with Compound II or as a reaction product of an oxidase-type reaction involving dihydroxyfumaric acid.","Characterization of the catalytic parameters of bromoperoxidase showed that the enzyme is capable of catalyzing chloride, bromide and iodide ion oxidation. The bromide and iodide oxidation reactions follow similar pH-rate profile equations and have pH optima near ph 6-7. Chloride oxidations follow a second pH-rate profile equation and have pH optima near pH 4. Kinetics of bromide ion oxidation demonstrated that monochlorodimedone (MCD) bromination catalyzed by bromoperoxidase involves tribromide ion formation. The bromide enhanced catalase-type reaction resulting from the catalytic degradation of hydrogen peroxide by bromoperoxidase was also shown to involve tribromide ion formation. Chloride ion oxidation was demonstrated by the isolation of labeled {('36)Cl}-dichlorodimedone synthesized by bromoperoxidase, MCD, peroxide, and Na('36)Cl. Similar chloride enhanced reactions were observed for 2-thiouracil oxidation and the catalase-type reaction. Compound III accumulates during the peroxidative and MCD bromination reactions catalyzed by bromoperoxidase. The accumulation of Compound III greatly affects the reaction rates for the above reactions.","Studies of the ferrous state of bromoperoxidase demonstrated that the enzyme exists as two reduced forms. Similar behavior was observed for the ferrous-carbonmonoxy complexes as well. The ferrous-carbonmonoixy complexes did not show a P-450 type spectrum but rather spectra similar to those observed for peroxidases containing a proximal imidazole ligand. Stepwise reductions of bromoperoxidase showed complicated reduction properties for the enzyme.","Made available in DSpace on 2014-12-15T23:43:49Z (GMT). No. of bitstreams: 1 8502234.pdf: 5235724 bytes, checksum: a778a8ca398330bde19649277781fc68 (MD5) Previous issue date: 1984","Embargo set by: Seth Robbins for item 70703 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","212 p.","Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1984."]},{"key":"dc:title","label":"Title","values":["Characterization of a Bromoperoxidase From the Marine Algae Penicillus Capitatus"]}]}],"canonical_facts":{"dc:creator":["Manthey, John Anthony"],"dc:date":["2014-12-15T23:43:49Z","10000-01-01","1984"],"dc:description":["The soluble emzyme bromperoxidase isolated from the marine green algae P. capitatus is capable of catalyzing halide oxiations while in the presence of peroxide. Protein purification and characterization of this enzyme showed that the prosthetic group is ferric protoporphyrin IX and that the enzyme consists of two equal molecular weight subunits whose combined weight is approximately 100,000. Bromoperoxidase contains no detectable level of carbohydrate.","Initial characterization of the oxidized intermediates of bromoperoxidase which result from the protein's reaction with peroxide molecules shows that bromoperoxidase forms typical Compound I and Compound II species. Electron para-magnetic resonance (EPR) measurements failed to show any radical signal associated with Compound I. A third oxidized intermediate, termed Compound III forms as a result of the reaction of peroxide with Compound II or as a reaction product of an oxidase-type reaction involving dihydroxyfumaric acid.","Characterization of the catalytic parameters of bromoperoxidase showed that the enzyme is capable of catalyzing chloride, bromide and iodide ion oxidation. The bromide and iodide oxidation reactions follow similar pH-rate profile equations and have pH optima near ph 6-7. Chloride oxidations follow a second pH-rate profile equation and have pH optima near pH 4. Kinetics of bromide ion oxidation demonstrated that monochlorodimedone (MCD) bromination catalyzed by bromoperoxidase involves tribromide ion formation. The bromide enhanced catalase-type reaction resulting from the catalytic degradation of hydrogen peroxide by bromoperoxidase was also shown to involve tribromide ion formation. Chloride ion oxidation was demonstrated by the isolation of labeled {('36)Cl}-dichlorodimedone synthesized by bromoperoxidase, MCD, peroxide, and Na('36)Cl. Similar chloride enhanced reactions were observed for 2-thiouracil oxidation and the catalase-type reaction. Compound III accumulates during the peroxidative and MCD bromination reactions catalyzed by bromoperoxidase. The accumulation of Compound III greatly affects the reaction rates for the above reactions.","Studies of the ferrous state of bromoperoxidase demonstrated that the enzyme exists as two reduced forms. Similar behavior was observed for the ferrous-carbonmonoxy complexes as well. The ferrous-carbonmonoixy complexes did not show a P-450 type spectrum but rather spectra similar to those observed for peroxidases containing a proximal imidazole ligand. Stepwise reductions of bromoperoxidase showed complicated reduction properties for the enzyme.","Made available in DSpace on 2014-12-15T23:43:49Z (GMT). No. of bitstreams: 1 8502234.pdf: 5235724 bytes, checksum: a778a8ca398330bde19649277781fc68 (MD5) Previous issue date: 1984","Embargo set by: Seth Robbins for item 70703 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","212 p.","Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1984."],"dc:identifier":["http://hdl.handle.net/2142/70537","(UMI)AAI8502234"],"dc:subject":["Biophysics, General"],"dc:title":["Characterization of a Bromoperoxidase From the Marine Algae Penicillus Capitatus"],"dc:type":["text"],"thesis:degree_discipline":["Biochemistry"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Ph.D."],"thesis:institution_name":["University of Illinois at Urbana-Champaign"]},"updated_at":"2026-07-22T22:26:03Z"}