Spectral properties of a divinyl chlorophyll a harboring mutant of Synechocystis sp. PCC6803

Photosynth Res. 2013 Nov;117(1-3):245-55. doi: 10.1007/s11120-013-9877-3. Epub 2013 Jun 29.

Abstract

A divinyl chlorophyll (DV-Chl) a harboring mutant of Synechocystis sp. PCC 6803, in which chlorophyll species is replaced from monovinyl(normal)-Chl a to DV-Chl a, was characterized. The efficiency of light utilization for photosynthesis was decreased in the mutant. Absorption spectra at 77 K and their fourth derivative analyses revealed that peaks of each chlorophyll forms were blue-shifted by 1-2 nm, suggesting lowered stability of chlorophylls at their binding sites. This was also true both in PSI and PSII complexes. On the other hand, fluorescence emission spectra measured at 77 K were not different between wild type and the mutant. This indicates that the mode of interaction between chlorophyll and its binding pockets responsible for emitting fluorescence at 77 K is not altered in the mutant. P700 difference spectra of thylakoid membranes and PSI complexes showed that the spectrum in Soret region was red-shifted by 7 nm in the mutant. This is a characteristic feature of DV-Chl a. Microenvironments of iron-sulfur center of a terminal electron acceptor of PSI complex, P430, were practically the same as that of wild type.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Chlorophyll / chemistry
  • Chlorophyll / metabolism*
  • Electrons
  • Iron-Sulfur Proteins / metabolism
  • Mutation / genetics*
  • Photosynthesis
  • Photosystem I Protein Complex / metabolism
  • Photosystem II Protein Complex / metabolism
  • Spectrometry, Fluorescence
  • Synechocystis / metabolism*
  • Thylakoids / metabolism
  • Vinyl Compounds / chemistry
  • Vinyl Compounds / metabolism*

Substances

  • Iron-Sulfur Proteins
  • Photosystem I Protein Complex
  • Photosystem II Protein Complex
  • Vinyl Compounds
  • divinyl chlorophyll a
  • Chlorophyll