The open, the closed, and the empty: time-resolved fluorescence spectroscopy and computational analysis of RC-LH1 complexes from Rhodopseudomonas palustris.

نویسندگان

  • Sebastian R Beyer
  • Lars Müller
  • June Southall
  • Richard J Cogdell
  • G Matthias Ullmann
  • Jürgen Köhler
چکیده

We studied the time-resolved fluorescence of isolated RC-LH1 complexes from Rhodopseudomonas palustris as a function of the photon fluence and the repetition rate of the excitation laser. Both parameters were varied systematically over 3 orders of magnitude. On the basis of a microstate description we developed a quantitative model for RC-LH1 and obtained very good agreement between experiments and elaborate simulations based on a global master equation approach. The model allows us to predict the relative population of RC-LH1 complexes with the special pair in the neutral state or in the oxidized state P(+) and those complexes that lack a reaction center.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Identification of protein W, the elusive sixth subunit of the Rhodopseudomonas palustris reaction center-light harvesting 1 core complex

The X-ray crystal structure of the Rhodopseudomonas (Rps.) palustris reaction center-light harvesting 1 (RC-LH1) core complex revealed the presence of a sixth protein component, variably referred to in the literature as helix W, subunit W or protein W. The position of this protein prevents closure of the LH1 ring, possibly to allow diffusion of ubiquinone/ubiquinol between the RC and the cytoch...

متن کامل

Tracking energy transfer between light harvesting complex 2 and 1 in photosynthetic membranes grown under high and low illumination.

Energy transfer (ET) between B850 and B875 molecules in light harvesting complexes LH2 and LH1/RC (reaction center) complexes has been investigated in membranes of Rhodopseudomonas palustris grown under high- and low-light conditions. In these bacteria, illumination intensity during growth strongly affects the type of LH2 complexes synthesized, their optical spectra, and their amount of energet...

متن کامل

Uphill energy transfer in LH2-containing purple bacteria at room temperature

Uphill energy transfer in the LH2-containing purple bacteria Rhodopseudomonas acidophila, Rhodopseudomonas palustris, Rhodobacter sphaeroides, Chromatium vinosum and Chromatium purpuratum was studied by stationary fluorescence spectroscopy at room temperature upon selective excitation of the B800 pigments of LH2 and the B880 pigments of LH1 at 803 nm and 900 nm, respectively. The resulting fluo...

متن کامل

Refinement of the x-ray structure of the RC LH1 core complex from Rhodopseudomonas palustris by single-molecule spectroscopy.

A unique combination of single-molecule spectroscopy with numerical simulations has allowed us to achieve a refined structural model for the bacteriochlorophyll a (BChl a) pigment arrangement in reaction center-light-harvesting 1 core complexes of Rhodopseudomonas palustris. Details in the optical spectra, such as spectral separation and mutual polarizations of spectral bands, are compared with...

متن کامل

Nanodissection and high-resolution imaging of the Rhodopseudomonas viridis photosynthetic core complex in native membranes by AFM. Atomic force microscopy.

In photosynthesis, highly organized multiprotein assemblies convert sunlight into biochemical energy with high efficiency. A challenge in structural biology is to analyze such supramolecular complexes in native membranes. Atomic force microscopy (AFM) with high lateral resolution, high signal-to-noise ratio, and the possibility to nanodissect biological samples is a unique tool to investigate m...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • The journal of physical chemistry. B

دوره 119 4  شماره 

صفحات  -

تاریخ انتشار 2015