{"id":{"repo_id":"texas-state","oai_identifier":"oai:digital.library.txst.edu:10877/6979"},"canonical_url":"https://search.dev.ndltd.org/etd/texas-state/oai:digital.library.txst.edu:10877/6979","repository":{"repo_id":"texas-state","name":"Texas State University","base_url":"https://digital.library.txst.edu/server/oai/request"},"display":{"title":"Purification, Characterization, and Active Site Studies of 2-(2'-Hydroxyphenyl) Benzenesulfinate Desulfinase (DSZB) from Nocardia Asteroides Sp. Strain A3H1","abstract":"Dibenzophene (DBT) and its complex heterocyclic derivatives comprise most of the sulfur that contaminates fossil fuels. The 2-(2´-hydroxyphenyl) benzenesulfinate desulfinase (DszB) enzyme metabolize sulfur from DBT compounds. DszB, one of the four enzymes of the desulfurizing pathway, catalyzes the carbon-sulfur bond cleavage in the last, and rate limiting step. The wildtype A3H1-DszB and the recombinant A3H1- R84Q-Y24Fand A3H1-R84Q-C27S DszBs from Nocarida asteroides sp. strain A3H1 were purified and characterized. The A3H1-R84Q-C27S- DszB was inactive. The temperature and pH optima for wildtype and A3H1-R84Q-Y24F DszBs were 35 ˚C and 8.5, respectively; the Km and kcat were 3.15 ± 0.74 µM and 1.24 ± 0.054 min-1, and 51.25 ± 0.96 µM and 4.33 ± 0.67 min-1, respectively. Overall, the A3H1-DszB showed a slower turnover rate and a moderately lower specificity for substrate when compared to the other DszB homologs referenced in this study. The mutant A3H1-R84Q-Y24F-DszB revealed that the enzyme was more susceptible to inhibition than the wildtype. Both DszBs were inhibited by 2,2-biphenol. Significant inhibition by a mixture of HBP and sulfite was observed in both enzymes.","abstract_html":"Dibenzophene (DBT) and its complex heterocyclic derivatives comprise most of the sulfur that contaminates fossil fuels. The 2-(2´-hydroxyphenyl) benzenesulfinate desulfinase (DszB) enzyme metabolize sulfur from DBT compounds. DszB, one of the four enzymes of the desulfurizing pathway, catalyzes the carbon-sulfur bond cleavage in the last, and rate limiting step. The wildtype A3H1-DszB and the recombinant A3H1- R84Q-Y24Fand A3H1-R84Q-C27S DszBs from Nocarida asteroides sp. strain A3H1 were purified and characterized. The A3H1-R84Q-C27S- DszB was inactive. The temperature and pH optima for wildtype and A3H1-R84Q-Y24F DszBs were 35 ˚C and 8.5, respectively; the Km and kcat were 3.15 ± 0.74 µM and 1.24 ± 0.054 min-1, and 51.25 ± 0.96 µM and 4.33 ± 0.67 min-1, respectively. Overall, the A3H1-DszB showed a slower turnover rate and a moderately lower specificity for substrate when compared to the other DszB homologs referenced in this study. The mutant A3H1-R84Q-Y24F-DszB revealed that the enzyme was more susceptible to inhibition than the wildtype. Both DszBs were inhibited by 2,2-biphenol. Significant inhibition by a mixture of HBP and sulfite was observed in both enzymes.","abstract_has_math":false,"creators":["Vaz, Jerusha C."],"institution":"Texas State University-San Marcos","degree_name":"Master of Science","degree_level":"Masters","degree_discipline":"Chemistry","degree_department":null,"school":null,"contributors":[],"advisors":["Watkins, Linette M."],"committee_chairs":[],"committee_members":["Lewis, Lysle Kevin","Booth, Rachell Eschette"],"year":2009,"date_issued":"2009-12","date_published":"2009-12","updated_at":"2026-07-27T21:22:53Z","subjects":["DszB","HPBS desulfinase","Nocarida asteroides","A3H1","DszB mechanism"],"languages":["en"],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://hdl.handle.net/10877/6979","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.advisor","label":"Advisor","values":["Watkins, Linette M."]},{"key":"dc:contributor.committeemember","label":"Committee Member","values":["Lewis, Lysle Kevin","Booth, Rachell Eschette"]},{"key":"dc:creator","label":"Author","values":["Vaz, Jerusha C."]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2018-02-19T22:26:22Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2018-02-19T22:26:22Z"]},{"key":"dc:date.issued","label":"Date","values":["2009-12"]},{"key":"dc:type","label":"Dc Type","values":["Thesis"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Chemistry"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Masters"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Master of Science"]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["Texas State University-San Marcos"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["DszB","HPBS desulfinase","Nocarida asteroides","A3H1","DszB mechanism"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language.iso","label":"Language (ISO)","values":["en"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.uri","label":"Identifier URI","values":["https://hdl.handle.net/10877/6979"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Dibenzophene (DBT) and its complex heterocyclic derivatives comprise most of the sulfur that contaminates fossil fuels. The 2-(2´-hydroxyphenyl) benzenesulfinate desulfinase (DszB) enzyme metabolize sulfur from DBT compounds. DszB, one of the four enzymes of the desulfurizing pathway, catalyzes the carbon-sulfur bond cleavage in the last, and rate limiting step. The wildtype A3H1-DszB and the recombinant A3H1- R84Q-Y24Fand A3H1-R84Q-C27S DszBs from Nocarida asteroides sp. strain A3H1 were purified and characterized. The A3H1-R84Q-C27S- DszB was inactive. The temperature and pH optima for wildtype and A3H1-R84Q-Y24F DszBs were 35 ˚C and 8.5, respectively; the Km and kcat were 3.15 ± 0.74 µM and 1.24 ± 0.054 min-1, and 51.25 ± 0.96 µM and 4.33 ± 0.67 min-1, respectively. Overall, the A3H1-DszB showed a slower turnover rate and a moderately lower specificity for substrate when compared to the other DszB homologs referenced in this study. The mutant A3H1-R84Q-Y24F-DszB revealed that the enzyme was more susceptible to inhibition than the wildtype. Both DszBs were inhibited by 2,2-biphenol. Significant inhibition by a mixture of HBP and sulfite was observed in both enzymes."]},{"key":"dc:format","label":"Dc Format","values":["Text"]},{"key":"dc:format.medium","label":"Dc Format Medium","values":["1 file (.pdf)"]},{"key":"dc:title","label":"Title","values":["Purification, Characterization, and Active Site Studies of 2-(2'-Hydroxyphenyl) Benzenesulfinate Desulfinase (DSZB) from Nocardia Asteroides Sp. Strain A3H1"]}]}],"canonical_facts":{"dc:contributor.advisor":["Watkins, Linette M."],"dc:contributor.committeemember":["Lewis, Lysle Kevin","Booth, Rachell Eschette"],"dc:creator":["Vaz, Jerusha C."],"dc:date.accessioned":["2018-02-19T22:26:22Z"],"dc:date.available":["2018-02-19T22:26:22Z"],"dc:date.issued":["2009-12"],"dc:description.abstract":["Dibenzophene (DBT) and its complex heterocyclic derivatives comprise most of the sulfur that contaminates fossil fuels. The 2-(2´-hydroxyphenyl) benzenesulfinate desulfinase (DszB) enzyme metabolize sulfur from DBT compounds. DszB, one of the four enzymes of the desulfurizing pathway, catalyzes the carbon-sulfur bond cleavage in the last, and rate limiting step. The wildtype A3H1-DszB and the recombinant A3H1- R84Q-Y24Fand A3H1-R84Q-C27S DszBs from Nocarida asteroides sp. strain A3H1 were purified and characterized. The A3H1-R84Q-C27S- DszB was inactive. The temperature and pH optima for wildtype and A3H1-R84Q-Y24F DszBs were 35 ˚C and 8.5, respectively; the Km and kcat were 3.15 ± 0.74 µM and 1.24 ± 0.054 min-1, and 51.25 ± 0.96 µM and 4.33 ± 0.67 min-1, respectively. Overall, the A3H1-DszB showed a slower turnover rate and a moderately lower specificity for substrate when compared to the other DszB homologs referenced in this study. The mutant A3H1-R84Q-Y24F-DszB revealed that the enzyme was more susceptible to inhibition than the wildtype. Both DszBs were inhibited by 2,2-biphenol. Significant inhibition by a mixture of HBP and sulfite was observed in both enzymes."],"dc:format":["Text"],"dc:format.medium":["1 file (.pdf)"],"dc:identifier.uri":["https://hdl.handle.net/10877/6979"],"dc:language.iso":["en"],"dc:subject":["DszB","HPBS desulfinase","Nocarida asteroides","A3H1","DszB mechanism"],"dc:title":["Purification, Characterization, and Active Site Studies of 2-(2'-Hydroxyphenyl) Benzenesulfinate Desulfinase (DSZB) from Nocardia Asteroides Sp. Strain A3H1"],"dc:type":["Thesis"],"thesis:degree_discipline":["Chemistry"],"thesis:degree_level":["Masters"],"thesis:degree_name":["Master of Science"],"thesis:institution_name":["Texas State University-San Marcos"]},"updated_at":"2026-07-27T21:22:53Z"}