Literature DB >> 306832

Activity and stability of the luciferase--flavin intermediate.

J E Becvar, S C Tu, J W Hastings.   

Abstract

A luciferase intermediate in the bacterial bioluminescence system, which is formed by reaction of enzyme with reduced flavin mononucleotide (FMNH2) and oxygen, is shown to emit light with added aldehyde under anaerobic conditions. The reaction with oxygen is thus effectively irreversible under the conditions used. The flavin chromophore has an absorption maximum at about 370 nm and the potential activity (bioluminescence yield) in the further reaction of the isolated intermediate with aldehyde is strictly proportional to the amount of this flavin chromophore.

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Year:  1978        PMID: 306832     DOI: 10.1021/bi00602a036

Source DB:  PubMed          Journal:  Biochemistry        ISSN: 0006-2960            Impact factor:   3.162


  5 in total

1.  Structure of the oxygen adduct intermediate in the bacterial luciferase reaction: C nuclear magnetic resonance determination.

Authors:  S Ghisla; J W Hastings; V Favaudon; J M Lhoste
Journal:  Proc Natl Acad Sci U S A       Date:  1978-12       Impact factor: 11.205

2.  Control of aldehyde synthesis in the luminous bacterium Beneckea harveyi.

Authors:  S Ulitzur; J W Hastings
Journal:  J Bacteriol       Date:  1979-02       Impact factor: 3.490

Review 3.  Bacterial bioluminescence: its control and ecological significance.

Authors:  K H Nealson; J W Hastings
Journal:  Microbiol Rev       Date:  1979-12

Review 4.  Biological diversity, chemical mechanisms, and the evolutionary origins of bioluminescent systems.

Authors:  J W Hastings
Journal:  J Mol Evol       Date:  1983       Impact factor: 2.395

5.  Characterization and postulated structure of the primary emitter in the bacterial luciferase reaction.

Authors:  M Kurfürst; S Ghisla; J W Hastings
Journal:  Proc Natl Acad Sci U S A       Date:  1984-05       Impact factor: 11.205

  5 in total

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