Environmental Biophysics and Molecular Ecology Program, Department of Marine and Coastal Sciences and Department of Earth and Planetary Sciences, Rutgers University, New Brunswick, NJ 08901, USA.
Center for Advanced Biotechnology and Medicine and the Department of Biochemistry and Molecular Biology, Robert Wood Johnson Medical School, Rutgers University, Piscataway, NJ 08854, USA.
Sci Adv. 2023 Mar 10;9(10):eabq1990. doi: 10.1126/sciadv.abq1990.
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.
祖先的代谢过程涉及氢化酶对分子氢的可逆氧化。现有的氢化酶酶是复杂的，由数百个氨基酸和多个辅助因子组成。我们设计了一个 13 个氨基酸的镍结合肽，能够在各种条件下从质子中产生大量的分子氢。该肽形成一个二镍簇，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、现存的蛋白质是新陈代谢的核心。这些实验结果表明，现代酶尽管非常复杂，但很可能是从早期地球上简单的肽前体进化而来的。
