{"title":"用时间分辨步进扫描FTIR光谱研究了脂质环境对细菌紫质质子化动力学的影响","authors":"Michael Jawurek, C. Glaubitz, K. Hauser","doi":"10.3233/BSI-160135","DOIUrl":null,"url":null,"abstract":"The membrane plays an important role in the structure and function of membrane proteins. We studied the influence of the lipid environment on the photocycle of the membrane protein bacteriorhodopsin (BR) with time-resolved step-scan FTIR spectroscopy. Proton transfer dynamics was monitored with microsecond time resolution for BR embedded in the native purple membrane as well as reconstituted into DOPC liposomes. We observed altered protonation dynamics of the Schiff base and the primary proton acceptor Asp85, revealing a faster rise as well as decay of the M state for BR surrounded by DOPC lipids. The purple membrane consists of a lipid composition that adapts better to the protein shape resulting in a stronger protein- membrane interaction as compared to the uniform DOPC lipid environment. Conformational dynamics and the correlated protonation dynamics are affected by the altered protein-membrane interaction explaining the faster photoreaction of BR in DOPC liposomes. Here we demonstrate the high sensitivity of the proton transfer dynamics to the lipid environment of BR.","PeriodicalId":44239,"journal":{"name":"Biomedical Spectroscopy and Imaging","volume":"94 1","pages":"167-174"},"PeriodicalIF":0.3000,"publicationDate":"2016-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3233/BSI-160135","citationCount":"3","resultStr":"{\"title\":\"Impact of the lipid environment on the protonation dynamics of bacteriorhodopsin studied with time-resolved step-scan FTIR spectroscopy\",\"authors\":\"Michael Jawurek, C. Glaubitz, K. Hauser\",\"doi\":\"10.3233/BSI-160135\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"The membrane plays an important role in the structure and function of membrane proteins. We studied the influence of the lipid environment on the photocycle of the membrane protein bacteriorhodopsin (BR) with time-resolved step-scan FTIR spectroscopy. Proton transfer dynamics was monitored with microsecond time resolution for BR embedded in the native purple membrane as well as reconstituted into DOPC liposomes. We observed altered protonation dynamics of the Schiff base and the primary proton acceptor Asp85, revealing a faster rise as well as decay of the M state for BR surrounded by DOPC lipids. The purple membrane consists of a lipid composition that adapts better to the protein shape resulting in a stronger protein- membrane interaction as compared to the uniform DOPC lipid environment. Conformational dynamics and the correlated protonation dynamics are affected by the altered protein-membrane interaction explaining the faster photoreaction of BR in DOPC liposomes. Here we demonstrate the high sensitivity of the proton transfer dynamics to the lipid environment of BR.\",\"PeriodicalId\":44239,\"journal\":{\"name\":\"Biomedical Spectroscopy and Imaging\",\"volume\":\"94 1\",\"pages\":\"167-174\"},\"PeriodicalIF\":0.3000,\"publicationDate\":\"2016-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.3233/BSI-160135\",\"citationCount\":\"3\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biomedical Spectroscopy and Imaging\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.3233/BSI-160135\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q4\",\"JCRName\":\"SPECTROSCOPY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biomedical Spectroscopy and Imaging","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.3233/BSI-160135","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"SPECTROSCOPY","Score":null,"Total":0}
Impact of the lipid environment on the protonation dynamics of bacteriorhodopsin studied with time-resolved step-scan FTIR spectroscopy
The membrane plays an important role in the structure and function of membrane proteins. We studied the influence of the lipid environment on the photocycle of the membrane protein bacteriorhodopsin (BR) with time-resolved step-scan FTIR spectroscopy. Proton transfer dynamics was monitored with microsecond time resolution for BR embedded in the native purple membrane as well as reconstituted into DOPC liposomes. We observed altered protonation dynamics of the Schiff base and the primary proton acceptor Asp85, revealing a faster rise as well as decay of the M state for BR surrounded by DOPC lipids. The purple membrane consists of a lipid composition that adapts better to the protein shape resulting in a stronger protein- membrane interaction as compared to the uniform DOPC lipid environment. Conformational dynamics and the correlated protonation dynamics are affected by the altered protein-membrane interaction explaining the faster photoreaction of BR in DOPC liposomes. Here we demonstrate the high sensitivity of the proton transfer dynamics to the lipid environment of BR.
期刊介绍:
Biomedical Spectroscopy and Imaging (BSI) is a multidisciplinary journal devoted to the timely publication of basic and applied research that uses spectroscopic and imaging techniques in different areas of life science including biology, biochemistry, biotechnology, bionanotechnology, environmental science, food science, pharmaceutical science, physiology and medicine. Scientists are encouraged to submit their work for publication in the form of original articles, brief communications, rapid communications, reviews and mini-reviews. Techniques covered include, but are not limited, to the following: • Vibrational Spectroscopy (Infrared, Raman, Teraherz) • Circular Dichroism Spectroscopy • Magnetic Resonance Spectroscopy (NMR, ESR) • UV-vis Spectroscopy • Mössbauer Spectroscopy • X-ray Spectroscopy (Absorption, Emission, Photoelectron, Fluorescence) • Neutron Spectroscopy • Mass Spectroscopy • Fluorescence Spectroscopy • X-ray and Neutron Scattering • Differential Scanning Calorimetry • Atomic Force Microscopy • Surface Plasmon Resonance • Magnetic Resonance Imaging • X-ray Imaging • Electron Imaging • Neutron Imaging • Raman Imaging • Infrared Imaging • Terahertz Imaging • Fluorescence Imaging • Near-infrared spectroscopy.