New insights into thiocyanate oxidation by human myeloperoxidase
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- 作者：Denise Schlorkea ; 1 ; Jö ; rg Flemmiga ; 1 ; Jana Gaua ; Paul G. Furtmü ; llerb ; Christian Obingerb ; Jü ; rgen Arnholda ; juergen.arnhold@medizin.uni-leipzig.de" class="auth_mail" title="E-mail the corresponding author
- 关键词：EPO ; eosinophil peroxidase ; LPO ; lactoperoxidase ; MPO ; myeloperoxidase ; NMR ; Nuclear magnetic resonance ; PMNs ; polymorphonuclear leukocytes
- 刊名：Journal of Inorganic Biochemistry
- 出版年：2016
- 出版时间：September 2016
- 年：2016
- 卷：162
- 期：Complete
- 页码：117-126
- 全文大小：1109 K
文摘
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SCN− is oxidised by the MPO-H2O2 (MPO: myeloperoxidase) system to hypothiocyanite.
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In the presence of H2O2, hypothiocyanite converts ferric MPO into Compound II.
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Hypothiocyanite alone converts ferric MPO into the MPO-cyanide complex.
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There is no one-electron oxidation of SCN− by Compound I of MPO.