Low-temperature femtosecond-resolution transient absorption spectroscopy of large-scale symmetry mutants of bacterial reaction centers

Biochemistry
S LinN W Woodbury

Abstract

Reaction centers isolated from three large-scale symmetry mutants sym0, sym2-1, and sym5-2 described in the previous article of this issue [Taguchi, A. K. W., Eastman, J. E., Gallo, D. M., Jr., Sheagley, E.. Xiao, W., & Woodbury, N. W. (1996) Biochemistry 35, 3175-3186] have been investigated by low-temperature ground state and ferntosecond-resolution transient absorption spectroscopy. All three of these large-scale symmetry mutants undergo electron transfer at 20 K. The mutants sym0 and sym5-2 have yields and dominant rates of charge separation comparable to wild type. However. the sym2-mutant shows a roughly 35%, quantum yield at this temperature, and the major kinetic component of the initial electron transfer is slower than wild type by nearly a factor of 100. The sym0 mutant showed substantial changes in the monomer bacteriochiorophyll ground state and transient spectra, and both sym0 sym2-1 showed changes in the bacteriopheophyll ground state and transient spectra. In particular, sym2-1 shows a small absorbance decrease in the region of the Qx band of the B side bacteriopheophytin which could be attributed to 10%-20% electron transfer along the B pathway.

Citations

Jul 27, 2001·Biochemical and Biophysical Research Communications·S Y ShinJ I Kim
Feb 27, 2014·Journal of the American Chemical Society·Palash K DuttaNeal W Woodbury
Oct 3, 2001·Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics·R Pincák, M Pudlak
Jan 2, 2020·Proceedings of the National Academy of Sciences of the United States of America·Philip D LaibleChristine Kirmaier
Jun 14, 2020·Biochimica Et Biophysica Acta. Bioenergetics·Alexey A ZabelinAnatoly Ya Shkuropatov

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