Multicopper manganese oxidase accessory proteins bind Cu and heme
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- 作者：Cristina N. Butterfielda ; 1 ; Lizhi Taob ; Kelly N. Chacó ; na ; 2 ; Thomas G. Spiroc ; Ninian J. Blackburna ; William H. Caseyd ; R. David Brittb ; Bradley M. Teboa ; tebob@ohsu.edu" class="auth_mail" title="E-mail the corresponding author
- 关键词：MCO ; multicopper oxidase ; EPR ; electron paramagnetic resonance ; EXAFS ; extended X-ray absorption spectroscopy ; UV&ndash ; vis ; UV visible ; SDS-PAGE ; sodium dodecyl sulfate polyacrylamide gel electrophoresis ; ICP-OES ; inductively coupled plasma-optical emission spectrometry ; MnxEF ; refers the product of the co-expression of genes mnxE and mnxF ; MnxEF3 ; refers to the H21A ; H80A ; and H82A modified protein
- 刊名：Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
- 出版年：2015
- 出版时间：December 2015
- 年：2015
- 卷：1854
- 期：12
- 页码：1853-1859
- 全文大小：871 K
文摘
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The MnxEF subunits of Bacillus PL-12 Mnx Mn oxidase oligomerize when co-expressed.
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EPR and XAS show at least one type 2 copper binds to a putative MnxEF hexamer.
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UV–vis shows low-spin heme binds to wild type and MnxEF triple His mutant.
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MnxEF is the first non-cytochrome protein to bind heme and type 2 copper.