Spectroscopic studies of Photosystem II in chlorophyll d -containing Acaryochloris marina

dc.contributor.authorRazeghifard, Mohammad
dc.contributor.authorChen, Min
dc.contributor.authorHughes, Joseph
dc.contributor.authorFreeman, Joel
dc.contributor.authorKrausz, Elmars
dc.contributor.authorWydrzynski, Thomas
dc.date.accessioned2015-12-13T22:53:56Z
dc.date.issued2005
dc.date.updated2015-12-11T11:00:59Z
dc.description.abstractPhotosystem II (PSII) electron transfer (ET) in the chlorophyll d-containing cyanobacterium Acaryochloris marina (A. marina) was studied by time-resolved electron paramagnetic resonance (EPR) spectroscopy at room temperature, chlorophyll fluorescence, and low-temperature optical spectroscopy. To maximize the ability to measure PSII ET in the intact cells of this organism, growth conditions were optimized to provide the highest specific O2 activity and the instrumental parameters for the EPR measurements of tyrosine Z (YZ) reduction were adjusted to give the best signal-to-noise over spectral resolution. Analysis of the YZ. reduction kinetics revealed that ET to the oxygen-evolving complex on the donor side of PSII in A, marina is indistinguishable from that in higher plants and other cyanobacteria. Likewise, the charge recombination kinetics between the first plastoquinone acceptor QA and the donor side of PSII monitored by the chlorophyll fluorescence decay on the seconds time scale are not significantly different between A. marina and non-chlorophyll d organisms, while low-temperature optical absorption spectroscopy identified the primary electron acceptor in A. marina as pheophytin a. The results indicate that, if the PSII primary electron donor in A. marina is made up of chlorophyll d instead of chlorophyll a, then there must be very different interactions with the protein environment to account for the ET properties, which are similar to higher plants and other cyanobacteria. Nevertheless, the water oxidation mechanism in A. marina is kinetically unaltered.
dc.identifier.issn0006-2960
dc.identifier.urihttp://hdl.handle.net/1885/82038
dc.publisherAmerican Chemical Society
dc.sourceBiochemistry
dc.subjectKeywords: Absorption spectroscopy; Electron spin resonance spectroscopy; Electron transitions; Fluorescence; Oxidation; Proteins; Signal to noise ratio; Cyanobacteria; Electron transfer (ET); Optical spectroscopy; Spectral resolution; Chlorophyll; chlorophyll; chlo
dc.titleSpectroscopic studies of Photosystem II in chlorophyll d -containing Acaryochloris marina
dc.typeJournal article
local.bibliographicCitation.issue33
local.bibliographicCitation.lastpage11187
local.bibliographicCitation.startpage11178
local.contributor.affiliationRazeghifard, Mohammad, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationChen, Min, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationHughes, Joseph, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationFreeman, Joel, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationKrausz, Elmars, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationWydrzynski, Thomas, College of Medicine, Biology and Environment, ANU
local.contributor.authoremailu4003719@anu.edu.au
local.contributor.authoruidRazeghifard, Mohammad, u4018863
local.contributor.authoruidChen, Min, u4081358
local.contributor.authoruidHughes, Joseph, u4003719
local.contributor.authoruidFreeman, Joel, u4045326
local.contributor.authoruidKrausz, Elmars, u8102117
local.contributor.authoruidWydrzynski, Thomas, u9114707
local.description.embargo2037-12-31
local.description.notesImported from ARIES
local.description.refereedYes
local.identifier.absfor060107 - Enzymes
local.identifier.absfor030606 - Structural Chemistry and Spectroscopy
local.identifier.ariespublicationMigratedxPub10338
local.identifier.citationvolume44
local.identifier.doi10.1021/bi048314c
local.identifier.scopusID2-s2.0-23944486368
local.identifier.uidSubmittedByMigrated
local.type.statusPublished Version

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