The [FeFe]-hydrogenase maturase HydF from Clostridium acetobutylicum contains a CO and CN- ligated iron cofactor
The [FeFe]-hydrogenase maturase HydF from Clostridium acetobutylicum contains a CO and CN- ligated iron cofactor
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DOI：
10.1016/j.febslet.2009.12.016
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发表时间：
2010-02-05
期刊：
影响因子：
3.5
通讯作者：
Happe, Thomas
中科院分区：
文献类型：
--
作者：
Czech, Ilka;Silakov, Alexey;Happe, Thomas
[FeFe]氢化酶活性位点（H-簇）的生物合成需要三个成熟因子，其各自的作用还不清楚。梭菌成熟酶（CaHydE、CaHydF和CaHydG）在其天然宿主丙酮丁醇梭菌中同源过表达。CaHydF能够激活莱茵衣藻[FeFe]氢化酶脱辅基蛋白（CrHy-dA 1（apo）），以几乎100%相比，天然的比放氢活性。根据电子顺磁共振谱和傅里叶变换红外光谱数据，建议存在[4Fe 4S]簇和CO和CN-配体配位的二铁簇。这项研究包含了第一个实验证据表明，双核部分的H-集群组装在HydF。(C)2009年欧洲生物化学学会联合会。Elsevier B. V.出版，保留所有权利。
Biosynthesis of the [FeFe] hydrogenases active site (H-cluster) requires three maturation factors whose respective roles are not understood yet. The clostridial maturation enzymes (CaHydE, CaHydF and CaHydG) were homologously overexpressed in their native host Clostridium acetobutylicum. CaHydF was able to activate Chlamydomonas reinhardtii [FeFe] hydrogenase apoprotein (CrHy-dA1(apo)) to almost 100% compared to the native specific hydrogen evolution activity. Based on electron paramagnetic resonance spectroscopy and Fourier-transform infrared spectroscopy data the existence of a [4Fe4S] cluster and a CO and CN- ligand coordinated di-iron cluster is suggested. This study contains the first experimental evidence that the bi-nuclear part of the H-cluster is assembled in HydF. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.