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Influence of solvent effects on Qy transitions in chlorophyll

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dc.contributor.author Smit, E
dc.contributor.author Prinsloo, LC
dc.contributor.author Nel, JM
dc.contributor.author Grobler, AF
dc.contributor.author Sparrow, RW
dc.date.accessioned 2011-07-22T11:00:13Z
dc.date.available 2011-07-22T11:00:13Z
dc.date.issued 2011-07
dc.identifier.citation Smit, E, Prinsloo, LC, Nel, JM, et al. 2011. Influence of solvent effects on Qy transitions in chlorophyll. South African Institute of Physics 2011 conference. Pretoria, 13-15 July 2011, pp. 1pp en_US
dc.identifier.uri http://hdl.handle.net/10204/5112
dc.description South African Institute of Physics 2011 conference. Pretoria, 13-15 July 2011 en_US
dc.description.abstract The most abundant and efficient light harvesting, energy transfer and transduction systems are found in nature within the process of photosynthesis. Although the processing sequences of an absorbed solar photon in the photosynthetic apparatus have been deciphered, the underlying physical basis of photosynthesis is not well understood yet. Our research aims to contribute to this understanding by characterising the level of organisation of the Light Harvesting II complexes (LHCII) and energy transfer systems when incorporated into artificial vesicles called PheroidTM. LHCII was extracted from spinach leaves in a 20 mM Tricine buffer to stabilise the proteins. Raman, FTIR and absorbance spectra of samples were compared. The Qy transitions of chlorophyll in the red (Qy) region of the absorption spectra appears to red-shift by 3.5 - 5.5 nm; indicating a possible change in organisation of the light harvesting system after incorporation into the PheroidTM. These shifts however could also be interpreted as bathochromic solvent effects due to the Tricine buffer. The objectives of this study were (1) to investigate whether the red-shifts were due to the Tricine buffer and (2) if so, whether the alternative use of a 20 mM K2HPO4 / KH2PO4 buffer could eliminate the bathochromic solvent effects. The Tricine buffer was dialysed out of the samples directly into a 20 mM K2HPO4 / KH2PO4 buffer to prevent denaturing of the LHCII proteins. Preliminary results indicated a lessening of the bathochromic effects with the K2HPO4 / KH2PO4 buffer. en_US
dc.language.iso en en_US
dc.relation.ispartofseries Workflow;6869
dc.subject Chlorophyll en_US
dc.subject Qy transitions en_US
dc.subject LHCII en_US
dc.title Influence of solvent effects on Qy transitions in chlorophyll en_US
dc.type Conference Presentation en_US
dc.identifier.apacitation Smit, E., Prinsloo, L., Nel, J., Grobler, A., & Sparrow, R. (2011). Influence of solvent effects on Qy transitions in chlorophyll. http://hdl.handle.net/10204/5112 en_ZA
dc.identifier.chicagocitation Smit, E, LC Prinsloo, JM Nel, AF Grobler, and RW Sparrow. "Influence of solvent effects on Qy transitions in chlorophyll." (2011): http://hdl.handle.net/10204/5112 en_ZA
dc.identifier.vancouvercitation Smit E, Prinsloo L, Nel J, Grobler A, Sparrow R, Influence of solvent effects on Qy transitions in chlorophyll; 2011. http://hdl.handle.net/10204/5112 . en_ZA
dc.identifier.ris TY - Conference Presentation AU - Smit, E AU - Prinsloo, LC AU - Nel, JM AU - Grobler, AF AU - Sparrow, RW AB - The most abundant and efficient light harvesting, energy transfer and transduction systems are found in nature within the process of photosynthesis. Although the processing sequences of an absorbed solar photon in the photosynthetic apparatus have been deciphered, the underlying physical basis of photosynthesis is not well understood yet. Our research aims to contribute to this understanding by characterising the level of organisation of the Light Harvesting II complexes (LHCII) and energy transfer systems when incorporated into artificial vesicles called PheroidTM. LHCII was extracted from spinach leaves in a 20 mM Tricine buffer to stabilise the proteins. Raman, FTIR and absorbance spectra of samples were compared. The Qy transitions of chlorophyll in the red (Qy) region of the absorption spectra appears to red-shift by 3.5 - 5.5 nm; indicating a possible change in organisation of the light harvesting system after incorporation into the PheroidTM. These shifts however could also be interpreted as bathochromic solvent effects due to the Tricine buffer. The objectives of this study were (1) to investigate whether the red-shifts were due to the Tricine buffer and (2) if so, whether the alternative use of a 20 mM K2HPO4 / KH2PO4 buffer could eliminate the bathochromic solvent effects. The Tricine buffer was dialysed out of the samples directly into a 20 mM K2HPO4 / KH2PO4 buffer to prevent denaturing of the LHCII proteins. Preliminary results indicated a lessening of the bathochromic effects with the K2HPO4 / KH2PO4 buffer. DA - 2011-07 DB - ResearchSpace DP - CSIR KW - Chlorophyll KW - Qy transitions KW - LHCII LK - https://researchspace.csir.co.za PY - 2011 T1 - Influence of solvent effects on Qy transitions in chlorophyll TI - Influence of solvent effects on Qy transitions in chlorophyll UR - http://hdl.handle.net/10204/5112 ER - en_ZA


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