Search citation statements
Paper Sections
Citation Types
Year Published
Publication Types
Relationship
Authors
Journals
The origin of homochirality in biological organisms remains an open question. Some suggest that its origin might be extraterrestrial, specifically due to the exposure of chiral molecules to circularly polarized photons in interstellar space, which could cause an initial population imbalance leading to the homochirality observed today. However, this extraterrestrial hypothesis has not been widely accepted, largely due to the belief that molecular optical rotatory dispersion is too insignificant to create the substantial imbalance required for homochirality. Here we report experimental evidence that specific conformers of neutral amino acids exhibit significant asymmetry in the chiral destroying dissociation rate induced by circularly polarized photons. The observed anisotropy factor for the lowest energy conformer of leucine was remarkably large, reaching 0.1�a factor of 13 times larger than observed for zwitterionic leucine in solid films, and nearly 40 times greater than the anisotropy reported in the electronic absorption spectrum of gas-phase leucine ensembles at room temperature. This significant finding indicates that even if reported anisotropy values in the electronic absorption spectrum are low, the dissociation asymmetry of certain conformers can still be substantial. An anisotropy factor of 0.1 could result in an initial enantiomeric excess exceeding 10%, even with a 90% extent of reaction. This discovery suggests that asymmetric photodissociation of amino acids may have been a crucial factor in the emergence of biological homochirality.
The origin of homochirality in biological organisms remains an open question. Some suggest that its origin might be extraterrestrial, specifically due to the exposure of chiral molecules to circularly polarized photons in interstellar space, which could cause an initial population imbalance leading to the homochirality observed today. However, this extraterrestrial hypothesis has not been widely accepted, largely due to the belief that molecular optical rotatory dispersion is too insignificant to create the substantial imbalance required for homochirality. Here we report experimental evidence that specific conformers of neutral amino acids exhibit significant asymmetry in the chiral destroying dissociation rate induced by circularly polarized photons. The observed anisotropy factor for the lowest energy conformer of leucine was remarkably large, reaching 0.1�a factor of 13 times larger than observed for zwitterionic leucine in solid films, and nearly 40 times greater than the anisotropy reported in the electronic absorption spectrum of gas-phase leucine ensembles at room temperature. This significant finding indicates that even if reported anisotropy values in the electronic absorption spectrum are low, the dissociation asymmetry of certain conformers can still be substantial. An anisotropy factor of 0.1 could result in an initial enantiomeric excess exceeding 10%, even with a 90% extent of reaction. This discovery suggests that asymmetric photodissociation of amino acids may have been a crucial factor in the emergence of biological homochirality.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.
customersupport@researchsolutions.com
10624 S. Eastern Ave., Ste. A-614
Henderson, NV 89052, USA
This site is protected by reCAPTCHA and the Google Privacy Policy and Terms of Service apply.
Copyright © 2024 scite LLC. All rights reserved.
Made with 💙 for researchers
Part of the Research Solutions Family.