Biochimica et Biophysica Acta - Bioenergetics
Biochimica et Biophysica Acta - Bioenergetics
5 years ago

Quinones in the A1 binding site in photosystem I studied using time-resolved FTIR difference spectroscopy

Quinones in the A1 binding site in photosystem I studied using time-resolved FTIR difference spectroscopy
Time-resolved step-scan FTIR difference spectroscopy at low temperature (77 K) has been used to study photosystem I particles with phylloquinone (2-methyl-3-phytyl-1,4-naphthaquinone) and menadione (2-methyl-1,4-naphthaquinone) incorporated into the A1 binding site. By subtracting spectra for PSI with phylloquinone incorporated from spectra for PSI with menadione incorporated a (menadione - phylloquinone) double difference spectrum was constructed. In the double difference spectrum bands associated with protein vibrational modes effectively cancel, and the bands in the spectrum are primarily associated with the neutral and reduced states of the two quinones in the A1 binding site. To aid in the assignment of bands in the experimental double difference spectrum, a double difference spectrum was calculated using three-layer ONIOM methods. The calculated and experimental spectra agree well, allowing unambiguous band assignments to be made. The ONIOM calculations show that both quinones in the A1 binding site are similarly oriented, with only a single hydrogen bond between the C4 =O quinone carbonyl group and the backbone NH group of a leucine residue. For the semi-quinone species, but not for the neutral species, this hydrogen bond appears to be very strong. Finally, we have for the first time been able to unmask and identify infrared difference bands associated with neutral naphthoquinone species occupying the A1 binding site in PSI.

Publisher URL: www.sciencedirect.com/science

DOI: S0005272817301044

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