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Fourier transform infrared difference spectroscopy (FTIR DS) has beenwidely used to study the structural details of electron transfer cofactors (and their binding sites) in many types of photosynthetic protein complexes. This review focuses in particular onwork that has been done to investigate the A1 cofactor in photosystemI photosynthetic reaction centers. A reviewof this subject area last appeared in 2006 [1], so onlywork undertaken since then will be covered here. Following light excitation of intact photosystem I particles the P700+A1 \ secondary radical pair state is formed within 100 ps. This state decays within 300 ns at room temperature, or 300 μs at 77 K. Given the short-lived nature of this state, it is not easily studied using “static” photo-accumulation FTIR difference techniques at either temperature. Time-resolved techniques are required. This article focuses on the use of time-resolved step-scan FTIR DS for the study of the P700+A1 \ state in intact photosystemI. Up until now, only our group has undertaken studies in this area. So, in this article, recent work undertaken in our lab is described, where we have used lowtemperature (77 K), microsecond time-resolved step-scan FTIR DS to study the P700+A1 \ state in photosystem I. In photosystemI a phylloquinone molecule occupies the A1 binding site. However, different quinones can be incorporated into the A1 binding site, and here work is described for photosystem I particles with plastoquinone-9, 2-phytyl naphthoquinone and 2-methyl naphthoquinone incorporated into the A1 binding site. Studies inwhich 18O isotope labeled phylloquinone has been incorporated into the A1 binding site are also discussed. To fully characterize PSI particles with different quinones incorporated into the A1 binding site nanosecond to millisecond visible absorption spectroscopy has been shown to be of considerable value, especially so when undertaken using identical samples under identical conditions to that used in time-resolved step-scan FTIRmeasurements. In this article the latest work that has been undertaken using both visible and infrared time resolved spectroscopies on the same sample will be described. Finally, vibrational spectroscopic data that has been obtained for phylloquinone in the A1 binding site in photosystem I is compared to corresponding data for ubiquinone in the QA binding site in purple bacterial reaction centers. This article is part of a Special Issue entitled: Vibrational spectroscopies and bioenergetic systems.


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Biochim Biophys Acta, 1847 (1), 55-68. DOI: 10.1016/j.bbabio.2014.07.014