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Photo-reduction of flavin mononucleotide to semiquinone form in LOV domain mutants of blue-light receptor phot from Chlamydomonas reinhardtii

Paper ID Volume ID Publish Year Pages File Format Full-Text
30519 44484 2007 12 PDF Available
Title
Photo-reduction of flavin mononucleotide to semiquinone form in LOV domain mutants of blue-light receptor phot from Chlamydomonas reinhardtii
Abstract

The photo-excitation dynamics of the mutants LOV1-C57S and LOV2-C250S of the LOV-domains of the phototropin photoreceptor phot from the green alga Chlamydomonas reinhardtii is investigated by absorption and fluorescence studies. The LOV domains fused to a maltose binding protein (MBP) are expressed in Escherichia coli. The mutants were studied under aerobic conditions in aqueous solution at pH 8. Blue-light exposure reduced the fully oxidized flavin mononucleotide, FMNox, to FMN semiquinone, FMNH, (quantum efficiency around 1%) which further reduced to FMN hydroquinone, FMNredH2 or FMNredH− (quantum efficiency ca. 3 × 10−5). In the dark both reduced forms recovered back to the oxidized form on a minute timescale. Besides photoreduction, blue-light photo-excitation of the mutants resulted in photoproduct formation (efficiency in the 2 × 10−4–10−3 range). Photo-reaction schemes for the mutants are discussed.

Keywords
LOV domain mutants; Flavin mononucleotide (FMN); Flavin semiquinone; Flavin hydroquinone; Photo-reduction; Blue-light photoreceptor; Chlamydomonas reinhardtii; Photo-cycle
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Photo-reduction of flavin mononucleotide to semiquinone form in LOV domain mutants of blue-light receptor phot from Chlamydomonas reinhardtii
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Photochemistry and Photobiology B: Biology - Volume 87, Issue 1, 2 April 2007, Pages 37–48
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
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Price was $35.95
You save - $31
Price after discount Only $4.95
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