Single-molecule paleoenzymology probes the chemistry of resurrected enzymes

A journey back in time is possible at the molecular level by reconstructing proteins from extinct organisms. Here we report the reconstruction, based on sequence predicted by phylogenetic analysis, of seven Precambrian thioredoxin enzymes (Trx), dating back between ~1.4 and ~4 billion years (Gyr). The reconstructed enzymes are up to 32° C more stable than modern enzymes and the oldest show significantly higher activity than extant ones at pH 5. We probed their mechanisms of reduction using single-molecule force spectroscopy. From the force-dependency of the rate of reduction of an engineered substrate, we conclude that ancient Trxs utilize chemical mechanisms of reduction similar to those of modern enzymes. While Trx enzymes have maintained their reductase chemistry unchanged, they have adapted over a 4 Gyr time span to the changes in temperature and ocean acidity that characterize the evolution of the global environment from ancient to modern Earth

Prebiotic Chemistry – Biochemistry – Emergence of Life (4.4–2 Ga)

This chapter is devoted to a discussion about the difficulties and even the impossibility to date the events that occurred during the transition from non-living matter to the first living cells. Nevertheless, the attempts to devise plausible scenarios accounting for the emergence of the main molecular devices and processes found in biology are presented including the role of nucleotides at early stages (RNA world). On the other hand, hypotheses on the development of early metabolisms, compartments and genetic encoding are also discussed in relation with their role in extant living organisms. The nature of the Last Common Ancestor is also presented as well as hypotheses on the evolution of viruses. The following sections constitute a collection of independent articles providing a general overview of these aspects. © Springer Science+Business Media B.V. 2006.SCOPUS: ar.jinfo:eu-repo/semantics/publishe