Document Detail

Oxygen triggering reversible modulation of Vibrio fischeri strain Y1 bioluminescence in vivo.
MedLine Citation:
PMID:  14974724     Owner:  NLM     Status:  MEDLINE    
Yellow-emitting Vibrio fischeri Y1 modulates its bioluminescence (BL) depending on the dissolved O2 concentration. On supplying O2 to the cells under anaerobiosis, the cells begin to emit striking yellow BL peaking around 535 nm. The enhanced yellow emission reverts reversibly to the original level after O2 is consumed. Moreover, the reversible rise and fall of the yellow emission occurs repeatedly in accord with the repeating cycles of aeration on and off. This indicates that an increase in the cellular amount of yellow fluorescent protein (YFP) is not an immediate cause of the yellow emission enhancement. One suggested explanation is that the activity of YFP originating from its highly fluorescent property is altered by redox interaction with the respiratory components, including the soluble cytochrome c. Under the O2-limited conditions, the cellular YFP molecules, in part, seem to lose the fluorescent property possibly because of being reduced via redox interaction with some respiratory components in reduced form. On stimulating aerobic respiration with O2 supply, the reduced YFP seems to retrieve its fluorescent property via oxidation possibly with both O2, diffused across the cell membrane, and ferricytochrome c, generated during the respiratory turnover. The suggested redox interactions seem primarily to cause the reversible BL modulation.
Hajime Karatani; Susumu Yoshizawa; Satoshi Hirayama
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Photochemistry and photobiology     Volume:  79     ISSN:  0031-8655     ISO Abbreviation:  Photochem. Photobiol.     Publication Date:  2004 Jan 
Date Detail:
Created Date:  2004-02-20     Completed Date:  2004-03-29     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0376425     Medline TA:  Photochem Photobiol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  120-5     Citation Subset:  IM    
Department of Polymer Science and Engineering, Kyoto Institute of Technology, Matsugasaki, Sakyo-ku, Kyoto, Japan.
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MeSH Terms
Bacterial Proteins / physiology
Carbonyl Cyanide m-Chlorophenyl Hydrazone / pharmacology
Cyanides / pharmacology
Luminescent Proteins / physiology
Oxygen Consumption / physiology*
Vibrio / drug effects,  physiology*
Reg. No./Substance:
0/Bacterial Proteins; 0/Cyanides; 0/Luminescent Proteins; 0/yellow fluorescent protein, Bacteria; 555-60-2/Carbonyl Cyanide m-Chlorophenyl Hydrazone

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

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