The Three-Dimensional Structure of [NiFeSe] Hydrogenase from Desulfovibrio vulgaris Hildenborough: A Hydrogenase without a Bridging Ligand in the Active Site in Its Oxidised, "as-Isolated" State
The Three-Dimensional Structure of [NiFeSe] Hydrogenase from Desulfovibrio vulgaris Hildenborough: A Hydrogenase without a Bridging Ligand in the Active Site in Its Oxidised, "as-Isolated" State
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DOI：
10.1016/j.jmb.2009.12.013
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发表时间：
2010-03-05
影响因子：
5.6
通讯作者：
Matias, Pedro M.
中科院分区：
文献类型：
--
作者：
Marques, Marta C.;Coelho, Ricardo;Matias, Pedro M.
氢是一种良好的能源载体，利用可再生资源生产氢是其广泛使用的必要条件。 [NiFeSe]氢化酶 (Hases) 是生物制氢的有吸引力的候选者，因为即使在适量的 O-2 存在下它们也能够实现高生产率，从而减少了对厌氧条件的要求。来自 Desulfovibrio vulgaris Hildenborough 的 [NiFeSe] Hase 的三维结构已在 2.04 埃分辨率下以其氧化的“分离状态”形式确定。值得注意的是，这是 [NiFe] fan-Lily 的氧化 Hase 的第一个结构，其活性位点不含氧化物桥配体。相反，观察到额外的硫原子结合 Ni 和 Se，形成 SeCys 构象，保护 NiFe 位点不与氧接触。这种结构提供了一些见解，可以解释这些酶的快速激活和 O-2 耐受性。 (C) 2009 Elsevier Ltd. 保留所有权利。
Hydrogen is a good energy vector, and its production from renewable sources is a requirement for its widespread use. [NiFeSe] hydrogenases, (Hases) are attractive candidates for the biological production of hydrogen because they are capable of high production rates even in the presence of moderate amounts of O-2, lessening the requirements for anaerobic conditions. The three-dimensional structure of the [NiFeSe] Hase from Desulfovibrio vulgaris Hildenborough has been determined in its oxidised "as-isolated" form at 2.04-angstrom resolution. Remarkably, this is the first structure of an oxidised Hase of the [NiFe] fan-Lily that does not contain an oxide bridging ligand at the active site. Instead, an extra sulfur atom is observed binding Ni and Se, leading to a SeCys conformation that shields the NiFe site from contact with oxygen. This structure provides several insights that may explain the fast activation and O-2 tolerance of these enzymes. (C) 2009 Elsevier Ltd. All rights reserved.