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WFRF:(Pascher A)
 

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LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00004211naa a2200325 4500
001oai:lup.lub.lu.se:7a5ad917-01f2-4f0a-af58-20c33eab014b
003SwePub
008160401s2005 | |||||||||||000 ||eng|
024a https://lup.lub.lu.se/record/1519582 URI
024a https://doi.org/10.1021/bi047473t2 DOI
040 a (SwePub)lu
041 a engb eng
042 9 SwePub
072 7a art2 swepub-publicationtype
072 7a ref2 swepub-contenttype
100a Polivka, Tomasu Lund University,Lunds universitet,Kemisk fysik,Enheten för fysikalisk och teoretisk kemi,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Chemical Physics,Physical and theoretical chemistry,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH4 aut0 (Swepub:lu)chph-tpo
2451 0a Spectroscopic properties of the carotenoid 3 '-hydroxyechinenone in the orange carotenoid protein from the cyanobacterium Arthrospira maxima
264 c 2005-02-18
264 1b American Chemical Society (ACS),c 2005
520 a The cyanobacterial water-soluble orange carotenoid binding protein (OCP) is an ideal system for study of the effects of protein environment on photophysical properties of carotenoids. It contains a single pigment, the carotenoid 3'-hydoxyechinenone (hECN). In this study, we focus on spectroscopic properties of hECN in solution and in the OCP, aiming to elucidate the spectroscopic effects of the carotenoid-protein interaction in the context of the function(s) of the OCP. The noncovalent binding of hECN to the OCP causes a conformational change in the hECN, leading to a prolongation of the effective conjugation length. This change is responsible for shortening of the S, lifetime from 6.5 ps in solution to 3.3 ps in the OCP. The conformational change and the hydrogen bonding via the carbonyl group of hECN result in stabilization of an intramolecular charge-transfer (ICT) state. No signs of the ICT state were found in hECN in solution, regardless of the solvent polarity; spectral bands in transient absorption spectra of OCP-bound hECN exhibit features typical for the ICT state. Application of global fitting analysis revealed further effects of binding hECN in the OCP. The S, state of hECN in the OCP decays with two time constants of 0.9 and 3.3 ps. Modeling of the excited-state processes suggests that these two components are due to two populations of hECN in the OCP that differ in the hydrogen bonding via the carbonyl group. These results support the hypothesis that the OCP functions as a photoprotective shield under excess light. Mechanistically, the broadening of the hECN absorption spectrum upon binding to OCP enhances filtering, effect of hECN. Furthermore, the binding-induced conformational change and activation of the ICT state that leads to a shortening of hECN lifetime effectively makes the protein-bound hECN a more effective energy dissipator.
650 7a NATURVETENSKAPx Biologix Biokemi och molekylärbiologi0 (SwePub)106022 hsv//swe
650 7a NATURAL SCIENCESx Biological Sciencesx Biochemistry and Molecular Biology0 (SwePub)106022 hsv//eng
700a Kerfeld, C A4 aut
700a Pascher, Torbjörnu Lund University,Lunds universitet,Kemisk fysik,Enheten för fysikalisk och teoretisk kemi,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Chemical Physics,Physical and theoretical chemistry,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH4 aut0 (Swepub:lu)chph-tpa
700a Sundström, Villyu Lund University,Lunds universitet,Kemisk fysik,Enheten för fysikalisk och teoretisk kemi,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Chemical Physics,Physical and theoretical chemistry,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH4 aut0 (Swepub:lu)chph-vs
710a Kemisk fysikb Enheten för fysikalisk och teoretisk kemi4 org
773t Biochemistryd : American Chemical Society (ACS)g 44:10, s. 3994-4003q 44:10<3994-4003x 0006-2960x 1520-4995
856u http://dx.doi.org/10.1021/bi047473ty FULLTEXT
8564 8u https://lup.lub.lu.se/record/151958
8564 8u https://doi.org/10.1021/bi047473t

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Polivka, Tomas
Kerfeld, C A
Pascher, Torbjör ...
Sundström, Villy
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NATURVETENSKAP
NATURVETENSKAP
och Biologi
och Biokemi och mole ...
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Biochemistry
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Lunds universitet

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