The primary donor of far-red photosystem II: ChlD1 or PD2?
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Judd, Martyna; Morton, Jennifer; Nürnberg, Dennis; Fantuzzi, Andrea; Rutherford, A William; Purchase, Robin; Cox, Nicholas; Krausz, Elmars
Description
Far-red light (FRL) Photosystem II (PSII) isolated from Chroococcidiopsis thermalis is studied using parallel analyses of low-temperature absorption, circular dichroism (CD) and magnetic circular dichroism (MCD) spectroscopies in conjunction with fluorescence measurements. This extends earlier studies (Nurnberg et al 2018 Science 360 (2018) 1210-1213). We confirm that the chlorophyll absorbing at 726 nm is the primary electron donor. At 1.8 K efficient photochemistry occurs when exciting at...[Show more]
dc.contributor.author | Judd, Martyna | |
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dc.contributor.author | Morton, Jennifer | |
dc.contributor.author | Nürnberg, Dennis | |
dc.contributor.author | Fantuzzi, Andrea | |
dc.contributor.author | Rutherford, A William | |
dc.contributor.author | Purchase, Robin | |
dc.contributor.author | Cox, Nicholas | |
dc.contributor.author | Krausz, Elmars | |
dc.date.accessioned | 2021-04-06T05:30:16Z | |
dc.identifier.issn | 0005-2728 | |
dc.identifier.uri | http://hdl.handle.net/1885/229678 | |
dc.description.abstract | Far-red light (FRL) Photosystem II (PSII) isolated from Chroococcidiopsis thermalis is studied using parallel analyses of low-temperature absorption, circular dichroism (CD) and magnetic circular dichroism (MCD) spectroscopies in conjunction with fluorescence measurements. This extends earlier studies (Nurnberg et al 2018 Science 360 (2018) 1210-1213). We confirm that the chlorophyll absorbing at 726 nm is the primary electron donor. At 1.8 K efficient photochemistry occurs when exciting at 726 nm and shorter wavelengths; but not at wavelengths longer than 726 nm. The 726 nm absorption peak exhibits a 21 ± 4 cm-1 electrochromic shift due to formation of the semiquinone anion, QA-. Modelling indicates that no other FRL pigment is located among the 6 central reaction center chlorins: PD1, PD2 ChlD1, ChlD2, PheoD1 and PheoD2. Two of these chlorins, ChlD1 and PD2, are located at a distance and orientation relative to QA- so as to account for the observed electrochromic shift. Previously, ChlD1 was taken as the most likely candidate for the primary donor based on spectroscopy, sequence analysis and mechanistic arguments. Here, a more detailed comparison of the spectroscopic data with exciton modelling of the electrochromic pattern indicates that PD2 is at least as likely as ChlD1 to be responsible for the 726 nm absorption. The correspondence in sign and magnitude of the CD observed at 726 nm with that predicted from modelling favors PD2 as the primary donor. The pros and cons of PD2 vs ChlD1 as the location of the FRL-primary donor are discussed. | |
dc.description.sponsorship | We recognize the support of the Australian Research Councilthrough grants DP110104565 and DP150103137 (EK), FT140100834(NC). This work was supported by BBSRC grants BB/L011506/1 andBB/R001383/1 (AWR, AF and DN) | |
dc.format.mimetype | application/pdf | |
dc.language.iso | en_AU | |
dc.publisher | Elsevier | |
dc.rights | © 2020 Elsevier B.V | |
dc.rights.uri | https://creativecommons.org/licenses/by-nc-nd/4.0/ | |
dc.source | Biochimica et biophysica acta. Bioenergetics | |
dc.subject | circular dichroism | |
dc.subject | electrochromic shift | |
dc.subject | exciton coupling | |
dc.subject | fluorescence | |
dc.subject | magnetic circular dichroism | |
dc.subject | photochemical charge separation | |
dc.subject | photochemistry | |
dc.subject | cyanobacteria | |
dc.subject | electron transport | |
dc.subject | photosynthetic reaction center complex proteins | |
dc.subject | photosystem ii protein complex | |
dc.subject | phycocyanin | |
dc.title | The primary donor of far-red photosystem II: ChlD1 or PD2? | |
dc.type | Journal article | |
local.identifier.citationvolume | 1861 | |
dc.date.issued | 2020-10-01 | |
local.publisher.url | https://www.elsevier.com/en-au | |
local.type.status | Published Version | |
local.contributor.affiliation | Judd, M., Research School of Chemistry, The Australian National University | |
local.contributor.affiliation | Morton, J., Research School of Chemistry, The Australian National University | |
local.contributor.affiliation | Purchase, R., Research School of Chemistry, The Australian National University | |
local.contributor.affiliation | Cox, N., Research School of Chemistry, The Australian National University | |
local.contributor.affiliation | Krausz, E., Research School of Chemistry, The Australian National University | |
dc.relation | http://purl.org/au-research/grants/arc/DP110104565 | |
dc.relation | http://purl.org/au-research/grants/arc/DP150103137 | |
dc.relation | http://purl.org/au-research/grants/arc/FT140100834 | |
local.identifier.essn | 1879-2650 | |
local.bibliographicCitation.issue | 10 | |
local.bibliographicCitation.startpage | 148248-1 | |
local.bibliographicCitation.lastpage | 148248-9 | |
local.identifier.doi | 10.1016/j.bbabio.2020.148248 | |
dcterms.accessRights | Open Access | |
dc.provenance | https://v2.sherpa.ac.uk/id/publication/12428..."The Accepted Version can be archived in an Institutional Repository. 12 Months. CC BY-NC-ND." from SHERPA/RoMEO site (as at 6/04/2021). | |
dc.rights.license | CC BY-NC-ND | |
Collections | ANU Research Publications |
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