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<p>Many cofactors share a molecular structure – adenosine monophosphate (AMP) – that otherwise occurs in nucleic acids. The presence of AMP in cofactors has presented an evolutionary puzzle. Is it a biochemical ‘handle’ that allows proteins to bind the cofactor more tightly, or a relic from a prebiotic time when cofactors arose? Using the example of nicotinamide adenine dinucleotide (NAD), we find a previously unknown property of its AMP handle. Experiments with hydrogen gas on mineral surfaces show that the handle-free nicotinamide mononucleotide (NMN) overreduces quickly, while NAD gets reduced specifically. The handle allows NAD to function in a hydrothermal, mineral-based setting, indicating that it is a form of protection against a harsh environment. Our findings uncover a specific functional role for the AMP moiety of NAD under environmental conditions capable of non-enzymatic NAD reduction, thereby identifying a structural element of a redox cofactor that is older than the enzymes using it.</p><p></p>

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Reduction of NAD and NMN on mineral surfaces with H2 reveals a functional role for the AMP moiety in a prebiotic context

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年10月30日

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  • Delfina P. Henriques Pereira,
  • Xiulan Xie,
  • Sarah V. Stewart,
  • Zainab Subrati,
  • Tuğçe Beyazay,
  • Nicole Paczia,
  • Jürgen Belz,
  • Kerstin Volz,
  • Valentina Erastova,
  • Harun Tüysüz,
  • Martina Preiner

摘要

Many cofactors share a molecular structure – adenosine monophosphate (AMP) – that otherwise occurs in nucleic acids. The presence of AMP in cofactors has presented an evolutionary puzzle. Is it a biochemical ‘handle’ that allows proteins to bind the cofactor more tightly, or a relic from a prebiotic time when cofactors arose? Using the example of nicotinamide adenine dinucleotide (NAD), we find a previously unknown property of its AMP handle. Experiments with hydrogen gas on mineral surfaces show that the handle-free nicotinamide mononucleotide (NMN) overreduces quickly, while NAD gets reduced specifically. The handle allows NAD to function in a hydrothermal, mineral-based setting, indicating that it is a form of protection against a harsh environment. Our findings uncover a specific functional role for the AMP moiety of NAD under environmental conditions capable of non-enzymatic NAD reduction, thereby identifying a structural element of a redox cofactor that is older than the enzymes using it.