Tuning Electron Flux through Nitrogenase with Methanogen Iron Protein Homologues
Tuning Electron Flux through Nitrogenase with Methanogen Iron Protein Homologues
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DOI：
10.1002/chem.201704378
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发表时间：
2017-11-16
影响因子：
4.3
通讯作者：
Hu, Yilin
中科院分区：
文献类型：
--
作者：
Hiller, Caleb J.;Stiebritz, Martin T.;Hu, Yilin
固氮酶使用一种称为Fe蛋白的还原酶组分将电子传递给其催化伙伴以进行底物还原。铁蛋白在催化中的重要作用使其成为在不干扰辅因子位点的情况下调节固氮酶的电子通量和酶活性的理想靶标。这项工作报告说，铁蛋白同源物的甲烷八叠球菌醋酸和棕色固氮菌的催化成分之间的杂交可以通过减少电子通量捕获底物CO。此外，同源性建模/计算机对接用于定义与实验确定的活性相关的组分蛋白质之间的结合能和特异性的标记物。这种基于同源物的方法可以进一步发展，以允许鉴定或设计同源固氮酶组分之间的杂交体，用于通过捕获底物/中间体或通过合成生物学进行固氮酶的转基因表达来进行固氮酶的机理研究。
Nitrogenase uses a reductase component called Fe protein to deliver electrons to its catalytic partner for substrate reduction. The essential role of Fe protein in catalysis makes it an ideal target for regulating the electron flux and enzymatic activity of nitrogenase without perturbing the cofactor site. This work reports that hybrids between the Fe protein homologs of Methanosarcina acetivorans and the catalytic components of Azotobacter vinelandii can trap substrate CO through reduced electron fluxes. In addition, homology modeling/in silico docking is used to define markers for binding energy and specificity between the component proteins that correlate with the experimentally determined activities. This homologue-based approach could be further developed to allow identification or design of hybrids between homologous nitrogenase components for mechanistic investigations of nitrogenase through capture of substrates/intermediates or for transgenic expression of nitrogenase through synthetic biology.