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| Item type: | Article | ||||
|---|---|---|---|---|---|
| Journal or Publication Title: | Biochemistry | ||||
| Volume: | 42 | ||||
| Number of Issue or Book Chapter: | 33 | ||||
| Page Range: | pp. 9854-9862 | ||||
| Date: | 2003 | ||||
| Additional Information (public): | CAN 139:256942 6-3 General Biochemistry 146-17-8D (FMN) Role: PEP (Physical, engineering or chemical process), PRP (Properties), PYP (Physical process), PROC (Process) (irreversible photoredn. of FMN in Phot photoreceptor LOV1 domain mutant) | ||||
| Institutions: | Chemistry and Pharmacy > Institut für Physikalische und Theoretische Chemie > Chair of Chemistry III - Physical Chemistry (Molecular Spectroscopy and Photochemistry) > Prof. Dr. Bernhard Dick | ||||
| Projects: | GRK 640 Sensory photoreceptors in natural and artificial systems | ||||
| Identification Number: |
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| Keywords: | Protein motifs (LOV (light, oxygen and voltage sensitive) domain,irreversible photoredn. of FMN in Phot photoreceptor LOV1 domain mutant); Phototropins, Role: PEP (Physical, engineering or chemical process), PRP (Properties), PYP (Physical process), PROC (Process) (LOV1 domain, C57M mutant irreversible photoredn. of FMN in Phot photoreceptor LOV1 domain mutant); Reduction, photochemical (irreversible photoredn. of FMN in Phot photoreceptor LOV1 domain mutant); Crystal structure; Total energy (of FMN photoadduct with Phot photoreceptor LOV1 domain mutant); Phot photoreceptor LOV1 domain FMN photoadduct | ||||
| Dewey Decimal Classification: | 500 Science > 570 Life sciences 500 Science > 540 Chemistry & allied sciences | ||||
| Status: | Published | ||||
| Refereed: | Yes, this version has been refereed | ||||
| Created at the University of Regensburg: | Yes | ||||
| Item ID: | 5560 |
Abstract
Phot photoreceptors make up an important protein family regulating biol. 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 FMN. Upon absorption of blue light, the LOV domains undergo a photocycle, transiently forming a covalent adduct of a cysteine residue and the FMN ...
Abstract
Phot photoreceptors make up an important protein family regulating biol. 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 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. The authors 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, irradn. 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 .ANG. resoln. 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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