Reduction of an Aldehyde by a NADH/Zn~(2+)-Dependent Redox Active Ribozyme

摘要

Redox chemistry is involved in various biological events, such as metabolism of biological molecules, detoxification, energy production, and regulation of protein functions. Although only protein enzymes in modern biology are able to catalyze redox reactions in concert with organic/inorganic cofactors, potential functions of RNA molecules in redox chemistry had been speculated in the context of the RNA world hypothesis. Specifically, the notion that RNA with cofactors might have been involved in ancient life before protein enzymes has been thus far supported by the following two facts: (1) circumstantial evidence that many organic cofactors such as nicotinamide adenine dinucleotide (NAD~+) and flavin adenine dinucleotide (FAD) consist of ribonucleotides3 and (2) experimental evidence that in vitro selection had yielded several RNA aptamers or RNA enzymes (ribozymes) that bind or react such nucleotide cofactors. However, no redox-active ribozyme was known until recently.