Excitonic Energy Landscape of the Y16F Mutant of the Chlorobium tepidum Fenna-Matthews-Olson (FMO) Complex: High Resolution Spectroscopic and Modeling Studies

J Phys Chem B. 2018 Apr 12;122(14):3734-3743. doi: 10.1021/acs.jpcb.7b11763. Epub 2018 Apr 3.

Abstract

We report high-resolution (low-temperature) absorption, emission, and nonresonant/resonant hole-burned (HB) spectra and results of excitonic calculations using a non-Markovian reduced density matrix theory (with an improved algorithm for parameter optimization in heterogeneous samples) obtained for the Y16F mutant of the Fenna-Matthews-Olson (FMO) trimer from the green sulfur bacterium Chlorobium tepidum. We show that the Y16F mutant is a mixture of FMO complexes with three independent low-energy traps (located near 817, 821, and 826 nm), in agreement with measured composite emission and HB spectra. Two of these traps belong to mutated FMO subpopulations characterized by significantly modified low-energy excitonic states. Hamiltonians for the two major subpopulations (Sub821 and Sub817) provide new insight into extensive changes induced by the single-point mutation in the vicinity of BChl 3 (where tyrosine Y16 was replaced with phenylalanine F16). The average decay time(s) from the higher exciton state(s) in the Y16F mutant depends on frequency and occurs on a picosecond time scale.

Publication types

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

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics*
  • Chlorobium / chemistry*
  • Chlorobium / genetics*
  • Energy Transfer*
  • Models, Molecular*
  • Multiprotein Complexes / chemistry*
  • Multiprotein Complexes / genetics*
  • Phenylalanine
  • Photosynthesis
  • Spectrometry, Fluorescence*
  • Tyrosine

Substances

  • Bacterial Proteins
  • Multiprotein Complexes
  • Tyrosine
  • Phenylalanine