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Elucidation of the heme active site electronic structure affecting the unprecedented nitrite dismutase activity of the ferriheme b proteins the nitrophorins

机译：阐明血红素活性位点电子结构会影响亚铁血红素b蛋白（亚硝酸盐）的前所未有的亚硝酸盐歧化酶活性

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Nitrophorins (NPs) catalyze the nitrite dismutation reaction that is unprecedented in ferriheme proteins. Despite progress in studying the reaction mechanism, fundamental issues regarding the correlation of the structural features with the nitrite dismutase activity of NPs remain elusive. On the other hand, it has been shown that the nitrite complexes of NPs are unique among those of the ferriheme proteins since some of their electron paramagnetic resonance (EPR) spectra show significant highly anisotropic low spin (HALS) signals with large gmax values over 3.2. The origin of HALS signals in ferriheme proteins or models is not well understood, especially in cases where axial ligands other than histidine are present. In this study several mutations were introduced in NP4. The related nitrite coordination and dismutation reaction were investigated. As a result, the EPR spectra of the NP–nitrite complexes were found to be tightly correlated with the extent of heme ruffling and protonation state of the proximal His ligand—dictated by an extended H-bonding network at the heme active site. Furthermore, it is established that the two factors are essential in determining the nitrite dismutase activity of NPs. These results may provide a valuable guide for identifying or designing novel heme proteins with similar activity.

机译：硝酸蛋白（NP）催化亚铁血红蛋白中前所未有的亚硝酸盐歧化反应。尽管在研究反应机理方面取得了进展，但是关于结构特征与NP的亚硝酸酯歧化酶活性之间关系的基本问题仍然难以捉摸。另一方面，已经证明，NPs的亚硝酸盐配合物在亚铁血红蛋白中是独特的，因为它们的某些电子顺磁共振（EPR）光谱显示出显着的高度各向异性的低自旋（HALS）信号，其gmax值超过3.2 。铁蛋白血红素蛋白或模型中HALS信号的起源还不太清楚，特别是在存在除组氨酸以外的轴向配体的情况下。在这项研究中，NP4中引入了几种突变。研究了相关的亚硝酸盐配位和歧化反应。结果，发现NP-亚硝酸盐配合物的EPR谱图与近端His配体的血红素起伏程度和质子化状态紧密相关，这取决于血红素活性位点的扩展H键网络。此外，已确定这两个因素对于确定NP的亚硝酸盐歧化酶活性至关重要。这些结果可能为鉴定或设计具有相似活性的新型血红素蛋白提供有价值的指导。

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期刊名称 Chemical Science
作者
Chunmao He; Hideaki Ogata; Wolfgang Lubitz;
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年(卷),期 2016(7),8
年度 2016
页码 5332–5340
总页数 9
原文格式 PDF
正文语种
中图分类生化遗传学;生化药理学;
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专利

1. Elucidation of the heme active site electronic structure affecting the unprecedented nitrite dismutase activity of the ferriheme b proteins, the nitrophorins [J] . He Chunmao, Ogata Hideaki, Lubitz Wolfgang Chemical science . 2016,第8期

机译：阐明血红素活性位点电子结构会影响亚铁血红素b蛋白（亚硝酸盐）的前所未有的亚硝酸盐歧化酶活性
2. Elucidation of the heme active site electronic structure affecting the unprecedented nitrite dismutase activity of the ferriheme b proteins, the nitrophorins [J] . Chunmao He, Hideaki Ogata, Wolfgang Lubitz Chemical science . 2016,第8期

机译：阐明血红素活性位电子结构影响亚铁血红素 b 蛋白（亚硝酸盐蛋白）前所未有的亚硝酸盐歧化酶活性

3. Elucidation of the heme active site electronic structure affecting the unprecedented nitrite dismutase activity of the ferriheme b proteins, the nitrophorins [J] . Chunmao He, Hideaki Ogata, Wolfgang Lubitz Chemical science . 2016,第8期

机译：阐明血红素活性位电子结构影响亚铁血红素 b 蛋白（亚硝酸盐蛋白）前所未有的亚硝酸盐歧化酶活性

4. The Interaction between the Ferriheme Protein Nitrophorin and Nitrite [C] . He, C., Ogata, European Biological Inorganic Chemistry Conference . 2010

机译：Ferriheme蛋白质硝基蛋白和亚硝酸盐之间的相互作用

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7. Assignment of ferriheme resonances for high- and low-spin forms of nitrophorin 3 by 1H and 13C NMR spectroscopy and comparison to nitrophorin 2: Heme pocket structural similarities and differences [O] . Tatiana Kh. Shokhireva, Robert E. Berry, Hongjun Zhang, 2008

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5. 修饰血红素提高血红蛋白类过氧化物酶活性 [J] . 凌辉生 ,李阳 ,封琳 . 生物加工过程 . 2011,第002期

6. 好氧反硝化细菌DN-2高活性亚硝酸盐还原酶活性和亚硝酸盐降解的研究 [C] . 洪秀娟 ,陈松 ,窦洁 . 第七届中国酶工程学术研讨会 . 2009

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机译：用于在疏水性活性蛋白中转化水溶性活性蛋白的方法，其用于制备具有定向活性的蛋白的单分子层，并且该装置包括将水溶性活性蛋白转化为疏水性活性蛋白的方法

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Elucidation of the heme active site electronic structure affecting the unprecedented nitrite dismutase activity of the ferriheme b proteins the nitrophorins

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