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Directly probing redox-linked quinones in photosystem II membrane fragments via UV resonance Raman scattering
Chen, Jun1,2; Yao, Mingdong1; Pagba, Cynthia V.3,4; Zheng, Yang1; Fei, Liping1; Feng, Zhaochi2; Barry, Bridgette A.3,4
KeywordCarbonyl Bond Photosynthesis Proton Transfer Electron Transfer Lipid Membrane Protein Dynamics
Source PublicationBIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
2015-06-01
DOI10.1016/j.bbabio.2015.03.002
Volume1847Issue:6-7Pages:558-564
Indexed BySCI
SubtypeArticle
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine
WOS SubjectBiochemistry & Molecular Biology ; Biophysics
WOS Research AreaBiochemistry & Molecular Biology ; Biophysics
WOS KeywordTRANSFORM INFRARED-SPECTROSCOPY ; ELECTRON-TRANSFER ; REACTION CENTERS ; SPECTRA ; ACCEPTOR ; 1,4-BENZOQUINONE ; REDUCTION ; DYNAMICS ; BINDING ; Q(A)
AbstractIn photosynthesis, photosystem II (PSII) harvests sunlight with bound pigments to oxidize water and reduce quinone to quinol, which serves as electron and proton mediators for solar-to-chemical energy conversion. At least two types of quinone cofactors in PSII are redox-linked: Q(A), and Q(B). Here, we for the first time apply 257-nm ultraviolet resonance Raman (UVRR) spectroscopy to acquire the molecular vibrations of plastoquinone (PQ) in PSII membranes. Owing to the resonance enhancement effect, the vibrational signal of PQ in PSII membranes is prominent. A strong band at 1661 cm(-1) is assigned to ring C=C/C=0 symmetric stretch mode (nu 8a mode) of PQ and a weak band at 469 cm(-1) to ring stretch mode. By using a pump-probe difference UVRR method and a sample jet technique, the signals of QA and QB can be distinguished. A frequency difference of 1.4 cm(-1) in nu 8a vibrational mode between QA and QB is observed, corresponding to similar to 86 mV redox potential difference imposed by their protein environment. In addition, there are other PQs in the PSII membranes. A negligible anharmonicity effect on their combination band at 2130 cm(-1) suggests that the 'other PQs' are situated in a hydrophobic environment. The detection of the 'other PQs' might be consistent with the view that another functional PQ cofactor (not Q(A) or Q(B)) exists in PSII. This UVRR approach will be useful to the study of quinone molecules in photosynthesis or other biological systems. (C) 2015 Elsevier B.V. All rights reserved.
Language英语
WOS IDWOS:000355054900007
Citation statistics
Cited Times:5[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://cas-ir.dicp.ac.cn/handle/321008/146246
Collection中国科学院大连化学物理研究所
Affiliation1.Chinese Acad Sci, Dalian Inst Chem Phys, Dalian Natl Lab Clean Energy, Dalian 116023, Peoples R China
2.Chinese Acad Sci, Dalian Inst Chem Phys, State Key Lab Catalysis, Dalian 116023, Peoples R China
3.Georgia Inst Technol, Sch Chem & Biochem, Atlanta, GA 30332 USA
4.Georgia Inst Technol, Petit Inst Bioengn & Biosci, Atlanta, GA 30332 USA
Recommended Citation
GB/T 7714
Chen, Jun,Yao, Mingdong,Pagba, Cynthia V.,et al. Directly probing redox-linked quinones in photosystem II membrane fragments via UV resonance Raman scattering[J]. BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS,2015,1847(6-7):558-564.
APA Chen, Jun.,Yao, Mingdong.,Pagba, Cynthia V..,Zheng, Yang.,Fei, Liping.,...&Barry, Bridgette A..(2015).Directly probing redox-linked quinones in photosystem II membrane fragments via UV resonance Raman scattering.BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS,1847(6-7),558-564.
MLA Chen, Jun,et al."Directly probing redox-linked quinones in photosystem II membrane fragments via UV resonance Raman scattering".BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS 1847.6-7(2015):558-564.
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