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  Irreversible photoreduction of flavin in a mutated Phot-LOV1 domain

Kottke, T., Dick, B., Fedorov, R., Schlichting, I., Deutzmann, R., & Hegemann, P. (2003). Irreversible photoreduction of flavin in a mutated Phot-LOV1 domain. Biochemistry, 42(33), 9854-9862. doi:10.1021/bi034863r.

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Genre: Zeitschriftenartikel
Alternativer Titel : Irreversible photoreduction of flavin in a mutated Phot-LOV1 domain

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 Urheber:
Kottke, Tilmann, Autor
Dick, Bernhard, Autor
Fedorov, Roman1, Autor           
Schlichting, Ilme1, Autor           
Deutzmann, Rainer, Autor
Hegemann, Peter, Autor
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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 Zusammenfassung: Phot photoreceptors make up an important protein family regulating biological processes in response to blue light. They contain two light, oxygen, and voltage sensitive (LOV) domains and a serine/threonine kinase domain. Both LOV domains noncovalently bind a flavin mononucleotide (FMN). Upon absorption of blue light, the LOV domains undergo a photocycle, transiently forming a covalent adduct of a cysteine residue and the FMN (LOV-390). The mechanism of formation of this flavin-thiol adduct is still unclear. We studied a mutant of the LOV1 domain from the green alga Chlamydomonas reinhardtii with a methionine replacing the reactive cysteine 57 (C57M). As in the wild type, irradiation leads to formation of a photoadduct, which, however, is irreversibly converted into a red absorbing species, C57M-675. On the basis of spectroscopic results and the 2.1 A resolution crystal structure, this highly unusual FMN species was assigned to a neutral flavin radical covalently attached to the apoprotein at the N(5) position. In contrast to other flavoprotein neutral radicals, C57M-675 is stable even under aerobic or denaturing conditions. Pathways for the photoinduced formation of the adduct are discussed for the C57M mutant as well as the wild-type LOV1 domain.

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Sprache(n): eng - English
 Datum: 2003-05-222003-08-012003-08-022003-08-26
 Publikationsstatus: Erschienen
 Seiten: 9
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Titel: Biochemistry
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: Columbus, Ohio : American Chemical Society
Seiten: - Band / Heft: 42 (33) Artikelnummer: - Start- / Endseite: 9854 - 9862 Identifikator: ISSN: 0006-2960
CoNE: https://pure.mpg.de/cone/journals/resource/954925384103