Low frequency magnetic fields modification on hydrogen peroxide oxidized myoglobin-isolate and mechanisms underlying the chain reaction process
•Increased magnetic field promoted H2O2 oxidation of myoglobin (Mb).•Magnetic fields of ≥ 9 mT changed the redox equivalents of Mb.•≥ 9 mT magnetic field shifted oxidation site from porphyrin ring to Mb skeleton.•Mb aggregation was affected by magnetic field-induced iron ion movement. The effects of...
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| Veröffentlicht in: | Food chemistry 2020-05, Vol.312, p.126069-126069, Article 126069 |
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| container_title | Food chemistry |
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| creator | Xia, Minquan Chen, Yinxia Ma, Jing Yin, Xiaoli Li, Zhenshun Xiong, Guangquan Wang, Lan Wu, Wenjin Sun, Weiqing Zhou, Yuanhua |
| description | •Increased magnetic field promoted H2O2 oxidation of myoglobin (Mb).•Magnetic fields of ≥ 9 mT changed the redox equivalents of Mb.•≥ 9 mT magnetic field shifted oxidation site from porphyrin ring to Mb skeleton.•Mb aggregation was affected by magnetic field-induced iron ion movement.
The effects of low frequency magnetic field (0–12 mT) on hydrogen peroxide oxidized myoglobin-isolate (MbI) were investigated. The results indicate that the primary target of the hydrogen peroxide oxidation was Met(FeIII)Mb, leading to the fall off of iron ions from the porphyrin ring. Additionally, the increased magnetic field (≥9 mT) enhanced the release of more iron ions to react with H2O2, giving rise to the production of more hydroxyl radicals and the shift of oxidation site from porphyrin ring to Mb skeleton. Moreover, the directional movement of iron ions induced by magnetic field caused the generation of local micro-electric field and the rearrangement of charged groups on the protein surface or near-surface, thus affecting Mb aggregation. Overall, the magnetic field interfered with the hydrogen peroxide chain reaction process, changed the redox equivalents of Mb, and shifted the oxidation sites of Mb. |
| doi_str_mv | 10.1016/j.foodchem.2019.126069 |
| format | Article |
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The effects of low frequency magnetic field (0–12 mT) on hydrogen peroxide oxidized myoglobin-isolate (MbI) were investigated. The results indicate that the primary target of the hydrogen peroxide oxidation was Met(FeIII)Mb, leading to the fall off of iron ions from the porphyrin ring. Additionally, the increased magnetic field (≥9 mT) enhanced the release of more iron ions to react with H2O2, giving rise to the production of more hydroxyl radicals and the shift of oxidation site from porphyrin ring to Mb skeleton. Moreover, the directional movement of iron ions induced by magnetic field caused the generation of local micro-electric field and the rearrangement of charged groups on the protein surface or near-surface, thus affecting Mb aggregation. Overall, the magnetic field interfered with the hydrogen peroxide chain reaction process, changed the redox equivalents of Mb, and shifted the oxidation sites of Mb.</description><identifier>ISSN: 0308-8146</identifier><identifier>EISSN: 1873-7072</identifier><identifier>DOI: 10.1016/j.foodchem.2019.126069</identifier><identifier>PMID: 31901702</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Circular dichroism (CD) spectroscopy ; Ferric Compounds - chemistry ; Hydrogen Peroxide - chemistry ; Hydrogen peroxide oxidation ; Hydroxyl Radical - chemistry ; Iron - chemistry ; Low frequency magnetic field ; Magnetic Fields ; Myoglobin - chemistry ; Myoglobin-isolate ; Oxidation-Reduction ; Porphyrins - chemistry</subject><ispartof>Food chemistry, 2020-05, Vol.312, p.126069-126069, Article 126069</ispartof><rights>2019 Elsevier Ltd</rights><rights>Copyright © 2019 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c368t-3c39794b5fbfddbbd402fb80c65e0bc1dfc2a65d974ad6a83893c4bd7d60e9aa3</citedby><cites>FETCH-LOGICAL-c368t-3c39794b5fbfddbbd402fb80c65e0bc1dfc2a65d974ad6a83893c4bd7d60e9aa3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0308814619322174$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31901702$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Xia, Minquan</creatorcontrib><creatorcontrib>Chen, Yinxia</creatorcontrib><creatorcontrib>Ma, Jing</creatorcontrib><creatorcontrib>Yin, Xiaoli</creatorcontrib><creatorcontrib>Li, Zhenshun</creatorcontrib><creatorcontrib>Xiong, Guangquan</creatorcontrib><creatorcontrib>Wang, Lan</creatorcontrib><creatorcontrib>Wu, Wenjin</creatorcontrib><creatorcontrib>Sun, Weiqing</creatorcontrib><creatorcontrib>Zhou, Yuanhua</creatorcontrib><title>Low frequency magnetic fields modification on hydrogen peroxide oxidized myoglobin-isolate and mechanisms underlying the chain reaction process</title><title>Food chemistry</title><addtitle>Food Chem</addtitle><description>•Increased magnetic field promoted H2O2 oxidation of myoglobin (Mb).•Magnetic fields of ≥ 9 mT changed the redox equivalents of Mb.•≥ 9 mT magnetic field shifted oxidation site from porphyrin ring to Mb skeleton.•Mb aggregation was affected by magnetic field-induced iron ion movement.
The effects of low frequency magnetic field (0–12 mT) on hydrogen peroxide oxidized myoglobin-isolate (MbI) were investigated. The results indicate that the primary target of the hydrogen peroxide oxidation was Met(FeIII)Mb, leading to the fall off of iron ions from the porphyrin ring. Additionally, the increased magnetic field (≥9 mT) enhanced the release of more iron ions to react with H2O2, giving rise to the production of more hydroxyl radicals and the shift of oxidation site from porphyrin ring to Mb skeleton. Moreover, the directional movement of iron ions induced by magnetic field caused the generation of local micro-electric field and the rearrangement of charged groups on the protein surface or near-surface, thus affecting Mb aggregation. Overall, the magnetic field interfered with the hydrogen peroxide chain reaction process, changed the redox equivalents of Mb, and shifted the oxidation sites of Mb.</description><subject>Circular dichroism (CD) spectroscopy</subject><subject>Ferric Compounds - chemistry</subject><subject>Hydrogen Peroxide - chemistry</subject><subject>Hydrogen peroxide oxidation</subject><subject>Hydroxyl Radical - chemistry</subject><subject>Iron - chemistry</subject><subject>Low frequency magnetic field</subject><subject>Magnetic Fields</subject><subject>Myoglobin - chemistry</subject><subject>Myoglobin-isolate</subject><subject>Oxidation-Reduction</subject><subject>Porphyrins - chemistry</subject><issn>0308-8146</issn><issn>1873-7072</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkctuEzEUhi0EomnhFSov2Uxqjye-7EAVBaRIbGBt-XKcOJqxgz0BhpfglXFIyxbJsqWj75xfxx9Ct5SsKaH87rAOOXu3h2ndE6rWtOeEq2doRaVgnSCif45WhBHZSTrwK3Rd64EQ0lj5El0xqggVpF-h39v8A4cC306Q3IIns0swR4dDhNFXPGUfQ3RmjjnhdvaLL3kHCR-h5J_RAz7f8Rd4PC15N2YbUxdrHs0M2KRWBbc3Kdap4lPyUMYlph2e94BbPSZcwLi_w48lO6j1FXoRzFjh9eN7g74-vP9y_7Hbfv7w6f7dtnOMy7ljjimhBrsJNnhvrR9IH6wkjm-AWEd9cL3hG6_EYDw3kknF3GC98JyAMobdoDeXuS237V5nPcXqYBxNgnyqumeMqV4KQRrKL6grudYCQR9LnExZNCX6LEMf9JMMfZahLzJa4-1jxslO4P-1Pf1-A95eAGibfo9QdHWxeQAfC7hZ-xz_l_EHr9-juQ</recordid><startdate>20200515</startdate><enddate>20200515</enddate><creator>Xia, Minquan</creator><creator>Chen, Yinxia</creator><creator>Ma, Jing</creator><creator>Yin, Xiaoli</creator><creator>Li, Zhenshun</creator><creator>Xiong, Guangquan</creator><creator>Wang, Lan</creator><creator>Wu, Wenjin</creator><creator>Sun, Weiqing</creator><creator>Zhou, Yuanhua</creator><general>Elsevier Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20200515</creationdate><title>Low frequency magnetic fields modification on hydrogen peroxide oxidized myoglobin-isolate and mechanisms underlying the chain reaction process</title><author>Xia, Minquan ; Chen, Yinxia ; Ma, Jing ; Yin, Xiaoli ; Li, Zhenshun ; Xiong, Guangquan ; Wang, Lan ; Wu, Wenjin ; Sun, Weiqing ; Zhou, Yuanhua</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c368t-3c39794b5fbfddbbd402fb80c65e0bc1dfc2a65d974ad6a83893c4bd7d60e9aa3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Circular dichroism (CD) spectroscopy</topic><topic>Ferric Compounds - chemistry</topic><topic>Hydrogen Peroxide - chemistry</topic><topic>Hydrogen peroxide oxidation</topic><topic>Hydroxyl Radical - chemistry</topic><topic>Iron - chemistry</topic><topic>Low frequency magnetic field</topic><topic>Magnetic Fields</topic><topic>Myoglobin - chemistry</topic><topic>Myoglobin-isolate</topic><topic>Oxidation-Reduction</topic><topic>Porphyrins - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Xia, Minquan</creatorcontrib><creatorcontrib>Chen, Yinxia</creatorcontrib><creatorcontrib>Ma, Jing</creatorcontrib><creatorcontrib>Yin, Xiaoli</creatorcontrib><creatorcontrib>Li, Zhenshun</creatorcontrib><creatorcontrib>Xiong, Guangquan</creatorcontrib><creatorcontrib>Wang, Lan</creatorcontrib><creatorcontrib>Wu, Wenjin</creatorcontrib><creatorcontrib>Sun, Weiqing</creatorcontrib><creatorcontrib>Zhou, Yuanhua</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Xia, Minquan</au><au>Chen, Yinxia</au><au>Ma, Jing</au><au>Yin, Xiaoli</au><au>Li, Zhenshun</au><au>Xiong, Guangquan</au><au>Wang, Lan</au><au>Wu, Wenjin</au><au>Sun, Weiqing</au><au>Zhou, Yuanhua</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Low frequency magnetic fields modification on hydrogen peroxide oxidized myoglobin-isolate and mechanisms underlying the chain reaction process</atitle><jtitle>Food chemistry</jtitle><addtitle>Food Chem</addtitle><date>2020-05-15</date><risdate>2020</risdate><volume>312</volume><spage>126069</spage><epage>126069</epage><pages>126069-126069</pages><artnum>126069</artnum><issn>0308-8146</issn><eissn>1873-7072</eissn><abstract>•Increased magnetic field promoted H2O2 oxidation of myoglobin (Mb).•Magnetic fields of ≥ 9 mT changed the redox equivalents of Mb.•≥ 9 mT magnetic field shifted oxidation site from porphyrin ring to Mb skeleton.•Mb aggregation was affected by magnetic field-induced iron ion movement.
The effects of low frequency magnetic field (0–12 mT) on hydrogen peroxide oxidized myoglobin-isolate (MbI) were investigated. The results indicate that the primary target of the hydrogen peroxide oxidation was Met(FeIII)Mb, leading to the fall off of iron ions from the porphyrin ring. Additionally, the increased magnetic field (≥9 mT) enhanced the release of more iron ions to react with H2O2, giving rise to the production of more hydroxyl radicals and the shift of oxidation site from porphyrin ring to Mb skeleton. Moreover, the directional movement of iron ions induced by magnetic field caused the generation of local micro-electric field and the rearrangement of charged groups on the protein surface or near-surface, thus affecting Mb aggregation. Overall, the magnetic field interfered with the hydrogen peroxide chain reaction process, changed the redox equivalents of Mb, and shifted the oxidation sites of Mb.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>31901702</pmid><doi>10.1016/j.foodchem.2019.126069</doi><tpages>1</tpages></addata></record> |
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| subjects | Circular dichroism (CD) spectroscopy Ferric Compounds - chemistry Hydrogen Peroxide - chemistry Hydrogen peroxide oxidation Hydroxyl Radical - chemistry Iron - chemistry Low frequency magnetic field Magnetic Fields Myoglobin - chemistry Myoglobin-isolate Oxidation-Reduction Porphyrins - chemistry |
| title | Low frequency magnetic fields modification on hydrogen peroxide oxidized myoglobin-isolate and mechanisms underlying the chain reaction process |
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