Photoreaction of the Cysteine S−H Group in the LOV2 Domain of Adiantum Phytochrome3

Phy3-LOV2 is the chromophore domain of a blue-light photoreceptor for tropic responses of plants. FMN is noncovalently bound to phy3-LOV2, and the protein structure is characteristic of the LOV (light-oxygen-voltage) domain. Primary photoreaction is considered to be adduct formation between FMN and...

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Veröffentlicht in:	Journal of the American Chemical Society 2002-10, Vol.124 (40), p.11840-11841
Hauptverfasser:	Iwata, Tatsuya, Tokutomi, Satoru, Kandori, Hideki
Format:	Artikel
Sprache:	eng
Schlagworte:	Adiantum - chemistry Analytical biochemistry: general aspects, technics, instrumentation Analytical, structural and metabolic biochemistry Biological and medical sciences Cysteine - chemical synthesis Fundamental and applied biological sciences. Psychology Photochemistry Phytochrome - chemistry Protein Structure, Tertiary Spectrophotometry, Infrared Spectrophotometry, Ultraviolet
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creator	Iwata, Tatsuya Tokutomi, Satoru Kandori, Hideki
description	Phy3-LOV2 is the chromophore domain of a blue-light photoreceptor for tropic responses of plants. FMN is noncovalently bound to phy3-LOV2, and the protein structure is characteristic of the LOV (light-oxygen-voltage) domain. Primary photoreaction is considered to be adduct formation between FMN and a cysteine, while deprotonation of the cysteine S−H group was suggested. On the basis of the infrared spectral analysis, however, we have shown that the cysteine of phy3-LOV2 is in the protonated S−H form, and not in the thiolate form in the ground state. Upon formation of S390, the S−H group disappears, presumably forming the adduct between FMN and Cys966. S390 can be trapped at 150 K, and the protein structure of S390 may not be changed drastically at 295 K.
doi_str_mv	10.1021/ja020834c
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FMN is noncovalently bound to phy3-LOV2, and the protein structure is characteristic of the LOV (light-oxygen-voltage) domain. Primary photoreaction is considered to be adduct formation between FMN and a cysteine, while deprotonation of the cysteine S−H group was suggested. On the basis of the infrared spectral analysis, however, we have shown that the cysteine of phy3-LOV2 is in the protonated S−H form, and not in the thiolate form in the ground state. Upon formation of S390, the S−H group disappears, presumably forming the adduct between FMN and Cys966. 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Am. Chem. Soc</addtitle><description>Phy3-LOV2 is the chromophore domain of a blue-light photoreceptor for tropic responses of plants. FMN is noncovalently bound to phy3-LOV2, and the protein structure is characteristic of the LOV (light-oxygen-voltage) domain. Primary photoreaction is considered to be adduct formation between FMN and a cysteine, while deprotonation of the cysteine S−H group was suggested. On the basis of the infrared spectral analysis, however, we have shown that the cysteine of phy3-LOV2 is in the protonated S−H form, and not in the thiolate form in the ground state. Upon formation of S390, the S−H group disappears, presumably forming the adduct between FMN and Cys966. S390 can be trapped at 150 K, and the protein structure of S390 may not be changed drastically at 295 K.</description><subject>Adiantum - chemistry</subject><subject>Analytical biochemistry: general aspects, technics, instrumentation</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Cysteine - chemical synthesis</subject><subject>Fundamental and applied biological sciences. 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Psychology</topic><topic>Photochemistry</topic><topic>Phytochrome - chemistry</topic><topic>Protein Structure, Tertiary</topic><topic>Spectrophotometry, Infrared</topic><topic>Spectrophotometry, Ultraviolet</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Iwata, Tatsuya</creatorcontrib><creatorcontrib>Tokutomi, Satoru</creatorcontrib><creatorcontrib>Kandori, Hideki</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of the American Chemical Society</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Iwata, Tatsuya</au><au>Tokutomi, Satoru</au><au>Kandori, Hideki</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Photoreaction of the Cysteine S−H Group in the LOV2 Domain of Adiantum Phytochrome3</atitle><jtitle>Journal of the American Chemical Society</jtitle><addtitle>J. Am. Chem. Soc</addtitle><date>2002-10-09</date><risdate>2002</risdate><volume>124</volume><issue>40</issue><spage>11840</spage><epage>11841</epage><pages>11840-11841</pages><issn>0002-7863</issn><eissn>1520-5126</eissn><coden>JACSAT</coden><abstract>Phy3-LOV2 is the chromophore domain of a blue-light photoreceptor for tropic responses of plants. FMN is noncovalently bound to phy3-LOV2, and the protein structure is characteristic of the LOV (light-oxygen-voltage) domain. Primary photoreaction is considered to be adduct formation between FMN and a cysteine, while deprotonation of the cysteine S−H group was suggested. On the basis of the infrared spectral analysis, however, we have shown that the cysteine of phy3-LOV2 is in the protonated S−H form, and not in the thiolate form in the ground state. Upon formation of S390, the S−H group disappears, presumably forming the adduct between FMN and Cys966. S390 can be trapped at 150 K, and the protein structure of S390 may not be changed drastically at 295 K.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>12358514</pmid><doi>10.1021/ja020834c</doi><tpages>2</tpages></addata></record>
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subjects	Adiantum - chemistry Analytical biochemistry: general aspects, technics, instrumentation Analytical, structural and metabolic biochemistry Biological and medical sciences Cysteine - chemical synthesis Fundamental and applied biological sciences. Psychology Photochemistry Phytochrome - chemistry Protein Structure, Tertiary Spectrophotometry, Infrared Spectrophotometry, Ultraviolet
title	Photoreaction of the Cysteine S−H Group in the LOV2 Domain of Adiantum Phytochrome3
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