Mechanism by which untwisting of retinal leads to productive bacteriorhodopsin photocycle states
Relaxation of the twisted-retinal photoproduct state triggers proton-coupled reaction cycle in retinal proteins. Given the crowded protein environments in which the retinal resides, a key open question is whether the retinal relaxation path is governed by the intrinsic torsional properties of the re...
Gespeichert in:
| Hauptverfasser: | , , , , |
|---|---|
| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
2015
|
| In: |
The journal of physical chemistry. B, Biophysics, biomaterials, liquids, and soft matter
Year: 2014, Jahrgang: 119, Heft: 6, Pages: 2229-2240 |
| ISSN: | 1520-5207 |
| DOI: | 10.1021/jp505818r |
| Online-Zugang: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1021/jp505818r
|
| Verfasserangaben: | Tino Wolter, Marcus Elstner, Stefan Fischer, Jeremy C. Smith, and Ana-Nicoleta Bondar |
MARC
| LEADER | 00000caa a2200000 c 4500 | ||
|---|---|---|---|
| 001 | 1703439538 | ||
| 003 | DE-627 | ||
| 005 | 20230426114640.0 | ||
| 007 | cr uuu---uuuuu | ||
| 008 | 200703r20152014xx |||||o 00| ||eng c | ||
| 024 | 7 | |a 10.1021/jp505818r |2 doi | |
| 035 | |a (DE-627)1703439538 | ||
| 035 | |a (DE-599)KXP1703439538 | ||
| 035 | |a (OCoLC)1341344410 | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rda | ||
| 041 | |a eng | ||
| 084 | |a 29 |2 sdnb | ||
| 100 | 1 | |a Wolter, Tino |e VerfasserIn |0 (DE-588)1046971174 |0 (DE-627)777380110 |0 (DE-576)400292890 |4 aut | |
| 245 | 1 | 0 | |a Mechanism by which untwisting of retinal leads to productive bacteriorhodopsin photocycle states |c Tino Wolter, Marcus Elstner, Stefan Fischer, Jeremy C. Smith, and Ana-Nicoleta Bondar |
| 264 | 1 | |c 2015 | |
| 300 | |a 12 | ||
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a Computermedien |b c |2 rdamedia | ||
| 338 | |a Online-Ressource |b cr |2 rdacarrier | ||
| 500 | |a Published:September 7, 2014 | ||
| 500 | |a Gesehen am 03.07.2020 | ||
| 520 | |a Relaxation of the twisted-retinal photoproduct state triggers proton-coupled reaction cycle in retinal proteins. Given the crowded protein environments in which the retinal resides, a key open question is whether the retinal relaxation path is governed by the intrinsic torsional properties of the retinal or rather by the interactions of the retinal with protein and water groups. Here we address this question by performing systematic quantum mechanical/molecular mechanical molecular dynamics computations of retinal dynamics in bacteriorhodopsin at different temperatures, reaction path computations, and assessment of the vibrational fingerprints of the retinal molecule. The results demonstrate a complex dependence of the retinal dynamics and preferred geometry on temperature. As the temperature increases, the retinal dihedral angle samples values largely determined by its internal conformational energy. The protein environment shapes the energetics of retinal relaxation and provides hydrogen-bonding partners that stabilize the retinal geometry. | ||
| 534 | |c 2014 | ||
| 700 | 1 | |a Elstner, Marcus |e VerfasserIn |4 aut | |
| 700 | 1 | |a Fischer, Stefan |e VerfasserIn |0 (DE-588)1026232961 |0 (DE-627)726307378 |0 (DE-576)371534100 |4 aut | |
| 700 | 1 | |a Smith, Jeremy C. |e VerfasserIn |4 aut | |
| 700 | 1 | |a Bondar, Ana-Nicoleta |e VerfasserIn |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t The journal of physical chemistry. B, Biophysics, biomaterials, liquids, and soft matter |d Washington, DC : Americal Chemical Society, 1997 |g 119(2015), 6, Seite 2229-2240 |h Online-Ressource |w (DE-627)320450953 |w (DE-600)2006039-7 |w (DE-576)090889002 |x 1520-5207 |7 nnas |a Mechanism by which untwisting of retinal leads to productive bacteriorhodopsin photocycle states |
| 773 | 1 | 8 | |g volume:119 |g year:2015 |g number:6 |g pages:2229-2240 |g extent:12 |a Mechanism by which untwisting of retinal leads to productive bacteriorhodopsin photocycle states |
| 856 | 4 | 0 | |u https://doi.org/10.1021/jp505818r |x Verlag |x Resolving-System |z lizenzpflichtig |3 Volltext |
| 951 | |a AR | ||
| 992 | |a 20200703 | ||
| 993 | |a Article | ||
| 994 | |a 2015 | ||
| 998 | |g 1026232961 |a Fischer, Stefan |m 1026232961:Fischer, Stefan |d 700000 |d 708000 |e 700000PF1026232961 |e 708000PF1026232961 |k 0/700000/ |k 1/700000/708000/ |p 3 | ||
| 999 | |a KXP-PPN1703439538 |e 3695240512 | ||
| BIB | |a Y | ||
| SER | |a journal | ||
| JSO | |a {"title":[{"title_sort":"Mechanism by which untwisting of retinal leads to productive bacteriorhodopsin photocycle states","title":"Mechanism by which untwisting of retinal leads to productive bacteriorhodopsin photocycle states"}],"person":[{"role":"aut","display":"Wolter, Tino","roleDisplay":"VerfasserIn","given":"Tino","family":"Wolter"},{"display":"Elstner, Marcus","roleDisplay":"VerfasserIn","role":"aut","family":"Elstner","given":"Marcus"},{"family":"Fischer","given":"Stefan","display":"Fischer, Stefan","roleDisplay":"VerfasserIn","role":"aut"},{"given":"Jeremy C.","family":"Smith","role":"aut","display":"Smith, Jeremy C.","roleDisplay":"VerfasserIn"},{"given":"Ana-Nicoleta","family":"Bondar","role":"aut","roleDisplay":"VerfasserIn","display":"Bondar, Ana-Nicoleta"}],"note":["Published:September 7, 2014","Gesehen am 03.07.2020"],"type":{"media":"Online-Ressource","bibl":"article-journal"},"recId":"1703439538","language":["eng"],"origin":[{"dateIssuedKey":"2015","dateIssuedDisp":"2015"}],"id":{"eki":["1703439538"],"doi":["10.1021/jp505818r"]},"name":{"displayForm":["Tino Wolter, Marcus Elstner, Stefan Fischer, Jeremy C. Smith, and Ana-Nicoleta Bondar"]},"physDesc":[{"extent":"12 S."}],"relHost":[{"title":[{"partname":"Biophysics, biomaterials, liquids, and soft matter","title":"The journal of physical chemistry","title_sort":"journal of physical chemistry"}],"language":["eng"],"recId":"320450953","note":["Gesehen am 30.05.2023"],"disp":"Mechanism by which untwisting of retinal leads to productive bacteriorhodopsin photocycle statesThe journal of physical chemistry. B, Biophysics, biomaterials, liquids, and soft matter","type":{"bibl":"periodical","media":"Online-Ressource"},"titleAlt":[{"title":"The journal of physical chemistry <Washington, DC> / B"},{"title":"Condensed matter, materials, surfaces, interfaces & biophysical chemistry"}],"part":{"issue":"6","pages":"2229-2240","year":"2015","extent":"12","text":"119(2015), 6, Seite 2229-2240","volume":"119"},"pubHistory":["101.1997 -"],"name":{"displayForm":["American Chemical Society"]},"id":{"zdb":["2006039-7"],"eki":["320450953"],"issn":["1520-5207"]},"origin":[{"dateIssuedDisp":"1997-","dateIssuedKey":"1997","publisher":"Americal Chemical Society","publisherPlace":"Washington, DC"}],"physDesc":[{"extent":"Online-Ressource"}]}]} | ||
| SRT | |a WOLTERTINOMECHANISMB2015 | ||