Search results for "Reaction centre"

Single amino acids in the lumenal loop domain influence the stability of the major light-harvesting chlorophyll a/b complex.

2004

The major light-harvesting complex of photosystem II (LHCIIb) is one of the most abundant integral membrane proteins. It greatly enhances the efficiency of photosynthesis in green plants by binding a large number of accessory pigments that absorb light energy and conduct it toward the photosynthetic reaction centers. Most of these pigments are associated with the three transmembrane and one amphiphilic alpha helices of the protein. Less is known about the significance of the loop domains connecting the alpha helices for pigment binding. Therefore, we randomly exchanged single amino acids in the lumenal loop domain of the bacterially expressed apoprotein Lhcb1 and then reconstituted the muta…

Picosecond time-resolved study on the nature of high-energy-state quenching in isolated pea thylakoids different localization of zeaxanthin dependent…

1996

Abstract The influence of the transthylakoid proton gradient on the kinetics of picosecond fluorescence decay was examined using isolated pea thylakoids having high or low zeaxanthin contents. Fluorescence lifetime measurements were performed with open (Fo) and closed (Fm) PS II reaction centers. Zeaxanthin formation in membrane energized isolated thylakoids led to a marked decrease of the average fluorescence lifetime at both Fm and Fo. In contrast, when zeaxanthin synthesis was blocked by the inhibitor DTT, the fluorescence lifetime decrease was less pronounced in the Fm state and totally missing in the Fo state. Samples containing the uncoupler ammonium chloride did not exhinit any zeaxa…

Myoglobin embedded in saccharide amorphous matrices: water-dependent domains evidenced by small angle X-ray scattering

2010

We report Small Angle X-ray Scattering (SAXS) measurements performed on samples of carboxy-myoglobin (MbCO) embedded in low-water trehalose glasses. Results showed that, in such samples, "low-protein" trehalose-water domains are present, surrounded by a protein-trehalose-water background; such finding is supported by Infrared Spectroscopy (FTIR) measurements. These domains, which do not appear in the absence of the protein and in analogous sucrose systems, preferentially incorporate the incoming water at the onset of rehydration, and disappear following large hydration. This observation suggests that, in organisms under anhydrobiosis, analogous domains could play a buffering role against th…

Quantum Chemical Simulations of Excited-State Absorption Spectra of Photosynthetic Bacterial Reaction Center and Antenna Complexes

2011

The semiempirical ZINDO/S CIS configuration interaction method has been used to study the ground- and excited-state absorption spectra of wild type and heterodimer M202HL reaction centers from purple bacterium Rhodobacter sphaeroides as well as of peripheral LH2 and LH3 light harvesting complexes from purple bacterium Rhodopseudomonas acidophila. The calculations well reproduce the experimentally observed excited-state absorption spectra between 1000 and 17,000 cm(-1), despite the necessarily limited number of chromophores and protein subunits involved in the calculations. The electron density analysis reveals that the charge transfer between adjacent chromophores dominates the excited-stat…

The Mechanism of Photoinhibition of Spinach Thylakoids

1990

There is conflicting evidence as to wether D1-protein is the primary target of photoinhibition [1] or P680, the reaction centre of photo-system II [2]. The present paper desribes photoinhibition within a two step process consisting of an oxygen radical induced inactivation at the QB-site followed by damage to reaction centre II through the degradation of the D1-protein.

Studien zum Vorgang der Wasserstoffübertragung, 39. Langlebige Hydrierkatalysatoren durch kovalente Verknüpfung von Phosphin-Rhodium-Komplexen an Aer…

1976

Homogene Phosphin-Rhodium-Katalysatoren werden durch kovalente Bindung an ‘Aminoaerosil’ heterogenisiert. Die Abhangigkeit der Hydriergeschwindigkeit von der Entfernung der aktiven Zentren zur Oberflache, von der Temperatur, vom Losungsmittel und von der Struktur der eingesetzten Olefine wird untersucht. Studies on the Occurrence of Hydrogen Transfer, 39. — Long-Lived Hydrogenation Catalyst by Covalent Fixation of Phosphine-Rhodium-Complexes on the Surface of Aerosil 200 The covalent binding of hitherto homogeneous phosphine-rhodium catalysts to “Amino-aerosil” is described. The dependence of the rate of catalysed hydrogenation upon the distance between the reaction centre and the silica su…

1998

Reaction centers (RC) from the species Erythrobacter (Eb.) litoralis, Erythromonas (Em.) ursincola and Sandaracinobacter (S.) sibiricus have been purified by LDAO treatment of light-harvesting-reaction center complexes and DEAE chromatography. The content and overall organisation of the RCs' chromophores, determined by linear dichroism (LD) and absorption spectroscopy, are similar to those isolated from anaerobic photosynthetic bacteria. The redox properties of the primary electron donor are pH-independent and very similar to those determined for anaerobic photosynthetic bacteria with midpoint potential values equal to 445 (± 10), 475 and 510 mV for Eb. litoralis, S. sibiricus and Em. ursin…

Mössbauer spectroscopy on the reaction center of Rhodopseudomonas viridis

1992

Proteins called “reaction centers” (RC) can be isolated from many photosynthetic bacteria. They have one non-heme iron in a quinone acceptor region. The RC of Rhodopseudomonas viridis contains an additional tightly bound tetra-heme cytochrome c subunit. The electronic configuration of both cytochrome and the non-heme iron has been studied in the crystallized protein by Mossbauer spectroscopy at different redox potentials, pH-values, and with an addition of o-phenanthroline. At high potentials (Eh=+500mV) all heme irons are in the low spin Fe3+-state, and at low potential (Eh=−150mV) they are low spin Fe2+ with the same Mossbauer parameters for all hemes independent of pH. Redox titrations c…