Design of a minimal di-nickel hydrogenase peptide.
Design of a minimal di-nickel hydrogenase peptide.
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DOI：
10.1126/sciadv.abq1990
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发表时间：
2023-03-10
期刊：
影响因子：
13.6
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中科院分区：
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祖先的代谢过程涉及氢酶对氢分子的可逆氧化。现存的氢化酶是复杂的，包括数百个氨基酸和多个辅因子。我们设计了一种13个氨基酸的镍结合肽，能够在各种条件下从质子中稳健地产生分子氢。该肽形成二镍簇，其结构类似于[NiFe]氢化酶中的Ni-Fe簇和乙酰辅酶A合酶中的Ni-Ni簇，这两种古老的现存蛋白质对代谢至关重要。这些实验结果表明，尽管现代酶非常复杂，但它们可能是从早期地球上的简单肽前体进化而来的。小的金属结合肽可能是现代酶的前体。
Ancestral metabolic processes involve the reversible oxidation of molecular hydrogen by hydrogenase. Extant hydrogenase enzymes are complex, comprising hundreds of amino acids and multiple cofactors. We designed a 13–amino acid nickel-binding peptide capable of robustly producing molecular hydrogen from protons under a wide variety of conditions. The peptide forms a di-nickel cluster structurally analogous to a Ni-Fe cluster in [NiFe] hydrogenase and the Ni-Ni cluster in acetyl-CoA synthase, two ancient, extant proteins central to metabolism. These experimental results demonstrate that modern enzymes, despite their enormous complexity, likely evolved from simple peptide precursors on early Earth. Small metal-binding peptides were the likely precursors of modern enzymes.