Document Detail

Coherently wired light-harvesting in photosynthetic marine algae at ambient temperature.
MedLine Citation:
PMID:  20130647     Owner:  NLM     Status:  MEDLINE    
Photosynthesis makes use of sunlight to convert carbon dioxide into useful biomass and is vital for life on Earth. Crucial components for the photosynthetic process are antenna proteins, which absorb light and transmit the resultant excitation energy between molecules to a reaction centre. The efficiency of these electronic energy transfers has inspired much work on antenna proteins isolated from photosynthetic organisms to uncover the basic mechanisms at play. Intriguingly, recent work has documented that light-absorbing molecules in some photosynthetic proteins capture and transfer energy according to quantum-mechanical probability laws instead of classical laws at temperatures up to 180 K. This contrasts with the long-held view that long-range quantum coherence between molecules cannot be sustained in complex biological systems, even at low temperatures. Here we present two-dimensional photon echo spectroscopy measurements on two evolutionarily related light-harvesting proteins isolated from marine cryptophyte algae, which reveal exceptionally long-lasting excitation oscillations with distinct correlations and anti-correlations even at ambient temperature. These observations provide compelling evidence for quantum-coherent sharing of electronic excitation across the 5-nm-wide proteins under biologically relevant conditions, suggesting that distant molecules within the photosynthetic proteins are 'wired' together by quantum coherence for more efficient light-harvesting in cryptophyte marine algae.
Elisabetta Collini; Cathy Y Wong; Krystyna E Wilk; Paul M G Curmi; Paul Brumer; Gregory D Scholes
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Nature     Volume:  463     ISSN:  1476-4687     ISO Abbreviation:  Nature     Publication Date:  2010 Feb 
Date Detail:
Created Date:  2010-02-04     Completed Date:  2010-03-12     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0410462     Medline TA:  Nature     Country:  England    
Other Details:
Languages:  eng     Pagination:  644-7     Citation Subset:  IM    
Department of Chemistry, Institute for Optical Sciences and Centre for Quantum Information and Quantum Control, University of Toronto, 80 St George Street, Toronto, Ontario, M5S 3H6 Canada.
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MeSH Terms
Algal Proteins / chemistry,  metabolism
Cryptophyta / metabolism*,  radiation effects*
Light-Harvesting Protein Complexes / chemistry,  metabolism
Models, Molecular
Photosynthesis / physiology,  radiation effects*
Protein Conformation
Quantum Theory
Reg. No./Substance:
0/Algal Proteins; 0/Light-Harvesting Protein Complexes
Comment In:
Nature. 2010 Feb 4;463(7281):614-5   [PMID:  20130637 ]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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