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

Biochemistry. 1996 Mar 12;35(10):3187-96. doi: 10.1021/bi952196z.

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.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Cold Temperature
  • Light
  • Mutation
  • Oxidation-Reduction
  • Photosynthetic Reaction Center Complex Proteins / genetics
  • Photosynthetic Reaction Center Complex Proteins / metabolism*
  • Photosynthetic Reaction Center Complex Proteins / radiation effects
  • Rhodobacter capsulatus / genetics*
  • Spectrometry, Fluorescence / methods
  • Spectrophotometry / methods
  • Structure-Activity Relationship

Substances

  • Photosynthetic Reaction Center Complex Proteins