Hemoglobin peroxidase reaction of hemoglobin efficiently catalyzes oxidation of benzo[a]pyrene
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Keum, Haein | - |
dc.contributor.author | Kim, Juhee | - |
dc.contributor.author | Joo, Yong Hoon | - |
dc.contributor.author | Kang, Guyoung | - |
dc.contributor.author | Chung, Namhyun | - |
dc.date.accessioned | 2021-11-22T01:40:22Z | - |
dc.date.available | 2021-11-22T01:40:22Z | - |
dc.date.created | 2021-08-30 | - |
dc.date.issued | 2021-04 | - |
dc.identifier.issn | 0045-6535 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/128298 | - |
dc.description.abstract | Its high molecular weight endows benzo[a]pyrene (BaP) with strong adsorption to soil, causing serious soil contamination. Our previous study has reported that hemoglobin (Hb) is able to oxidize organic pollutants in the presence of H2O2. This present study showed that Hb catalytic mechanism for BaP oxidation was similar to that of lignin peroxidase. 2-Methyl-3-vinylmaleimide was confirmed as a major degradation intermediate of BaP by Hb catalysis. In addition, BaP was shown to be degraded by heme (Hm)-catalyzed reaction, suggesting that Hm of Hb is the essential catalytic center. Rate constants (k) for BaP oxidation by Hm-catalyzed reaction were 0.4954 h(-1). The major degradation intermediate by Hm-catalyzed reaction is 3,3',5,5'-tetramethylbiphenyl. While values of K-m and V-max of Hb and Hm are very similar, k(cat) values was 100 times higher with Hb than with Hm. But k(cat) value for Hb was much lower than that for lignin peroxidase H2. All the results above suggested that Hb-catalyzed reactions efficiently degrade BaP in aqueous condition. Thus, we suggest that Hb for oxygen carrier in blood could be employed as a biocatalyst (i.e., hemoglobin peroxidase) for BaP degradation in the environment, due to the high availability of Hb. (C) 2020 Elsevier Ltd. All rights reserved. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | PERGAMON-ELSEVIER SCIENCE LTD | - |
dc.title | Hemoglobin peroxidase reaction of hemoglobin efficiently catalyzes oxidation of benzo[a]pyrene | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Chung, Namhyun | - |
dc.identifier.doi | 10.1016/j.chemosphere.2020.128795 | - |
dc.identifier.scopusid | 2-s2.0-85095790624 | - |
dc.identifier.wosid | 000615571300012 | - |
dc.identifier.bibliographicCitation | CHEMOSPHERE, v.268 | - |
dc.relation.isPartOf | CHEMOSPHERE | - |
dc.citation.title | CHEMOSPHERE | - |
dc.citation.volume | 268 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Environmental Sciences & Ecology | - |
dc.relation.journalWebOfScienceCategory | Environmental Sciences | - |
dc.subject.keywordAuthor | Benzo[a]pyrene | - |
dc.subject.keywordAuthor | Biocatalytic reaction | - |
dc.subject.keywordAuthor | Heme | - |
dc.subject.keywordAuthor | Hemoglobin | - |
dc.subject.keywordAuthor | Peroxidation | - |
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.
145 Anam-ro, Seongbuk-gu, Seoul, 02841, Korea+82-2-3290-2963
COPYRIGHT © 2021 Korea University. All Rights Reserved.
Certain data included herein are derived from the © Web of Science of Clarivate Analytics. All rights reserved.
You may not copy or re-distribute this material in whole or in part without the prior written consent of Clarivate Analytics.