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

Su Lin, Weizhong Xiao, J. Elizabeth Eastman, Aileen K W Taguchi, Neal Woodbury

Research output: Contribution to journalArticle

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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., and Woodbury, N. W. (1996) Biochemistry 35, 3175-3186] have been investigated by low-temperature ground state and femtosecond-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 sym2-1 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 bacteriochlorophyll ground state and transient spectra, and both sym0 and sym2-1 showed changes in the bacteriopheophytin ground state and transient spectra. In particular, sym2-1 shows a small absorbance decrease in the region of the Q(x) band of the B side bacteriopheophytin which could be attributed to 10%-20% electron transfer along the B pathway.

Original languageEnglish (US)
Pages (from-to)3187-3196
Number of pages10
JournalBiochemistry
Volume35
Issue number10
DOIs
StatePublished - Mar 12 1996

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Absorption spectroscopy
Ground state
Spectrum Analysis
Electrons
Temperature
Bacteriochlorophylls
Biochemistry
Quantum yield
Monomers
Kinetics
bacteriopheophytin

ASJC Scopus subject areas

  • Biochemistry

Cite this

Low-temperature femtosecond-resolution transient absorption spectroscopy of large-scale symmetry mutants of bacterial reaction centers. / Lin, Su; Xiao, Weizhong; Eastman, J. Elizabeth; Taguchi, Aileen K W; Woodbury, Neal.

In: Biochemistry, Vol. 35, No. 10, 12.03.1996, p. 3187-3196.

Research output: Contribution to journalArticle

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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., and Woodbury, N. W. (1996) Biochemistry 35, 3175-3186] have been investigated by low-temperature ground state and femtosecond-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 sym2-1 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 bacteriochlorophyll ground state and transient spectra, and both sym0 and sym2-1 showed changes in the bacteriopheophytin ground state and transient spectra. In particular, sym2-1 shows a small absorbance decrease in the region of the Q(x) band of the B side bacteriopheophytin which could be attributed to 10{\%}-20{\%} electron transfer along the B pathway.",
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