1. Reconstitution and exchange of quinones in the A1 site of Photosystem I. An electron spin polarization electron paramagnetic resonance study
- Author
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Seth W. Snyder, John Biggins, Marion C. Thurnauer, Richard R Rustandi, and James R. Norris
- Subjects
chemistry.chemical_classification ,Biophysics ,Analytical chemistry ,Cell Biology ,Photochemistry ,Photosystem I ,Biochemistry ,Acceptor ,Benzoquinone ,Naphthoquinone ,Quinone ,law.invention ,chemistry.chemical_compound ,Electron transfer ,chemistry ,law ,Electron paramagnetic resonance ,Alkyl - Abstract
The electron spin polarized (ESP) electron paramagnetic resonance (EPR) signal observed in spinach Photosystem I (PS I) particles was examined in preparations depleted of vitamin K 1 by solvent extraction, followed by reconstitution with a series of quinones and quinone analogues. The ESP EPR signal was previously attributed to a radicalpair that included vitaim K 1 − (Rustandi, R.R., et al. (1990) Biochemistry 29, 8030–8032) and, in addition, vitamin K 1 was assigned as the secondary acceptor A 1 in PS I (Snyder, S.W., et al. (1991) Proc. Natl. Acad. Sci. USA, 88, 9895–9896). The ESP EPR signal was observed in untreated PS I preparations, was not detected in the solvent-extracted PS I samples and was restored upon reconstitution using certain quinones. The ability to restore the ESP EPR signal was dependent upon two properties of the reconstituted acceptor. First, the solution reduction potential of the reconstituted acceptor must be more positive than about −750 mV where the solution reduction potential of vitamin K 1 is −710 mV. Second, the structure of the reconstituted acceptor requires either a minimum of two aromatic rings (i.e., naphthoquinone) or a benzoquinone (or larger) derivative substituted with an alkyl tail. A model was developed to describe both the requirements for electron transfer to A 1 and also previous results for electron transfer from A 1 − to the iron-sulfur centers (Biggins, J. (1990) Biochemistry 29, 7259–7264). When untreated PS I preparations were incubated with perdeuterated vitamin K 1 (DK 1 ) the endogenous K 1 was observed to exchange with DK 1 . The replacement rate was strongly dependent upon temperature (h-days at 4°C, min at 37°C) and upon illumination (min). Naphthoquinones lacking a long alkyl tail were unable to exchange with endogenous vitamin K 1 . Although no known physiological role exists for vitamin K 1 ejection from its A 1 binding site, the quinone appears to be somewhat labile. Direct exchange of vitamin K 1 with exogenously supplied quinones indicates that the PS I A 1 site might be a target for the design of new herbicides in green plants.
- Published
- 1992