Inorganic Fe2+ formation upon Fe-S protein thermodestruction in the membranes of thermophilic cyanobacteria: Mössbauer spectroscopy study.

A model description of the Mössbauer spectrum (80 K) of native membranes of the thermophilic cyanobacterium Synechococcus elongatus is suggested on the basis of the known values of quadrupole splitting (deltaE(Q)) and isomer shift (deltaFe) for the iron-containing components of the photosynthetic apparatus. Using this approach, we found that heating the membranes at 70-80 K results in a decrease of doublet amplitudes belonging to F(X), F(A), F(B) and ferredoxin and simultaneous formation of a new doublet with deltaE(Q) = 3.10 mm/s and delta-Fe = 1.

Effect of formate on Mössbauer parameters of the non-heme iron of PS II particles of cyanobacteria.

Mössbauer spectra were measured for PSII particles having an active water-splitting system. The particles were isolated from the thermophilic cyanobacterium Synechococcus elongatus enriched in 57Fe. The Mössbauer resonance absorption spectrum is a superposition of 3 doublets with the following quadrupole splitting and chemical shift: 1, delta = 0.

Mössbauer spectroscopy of iron metabolism and iron intracellular distribution in liver of rats.

Mössbauer spectroscopy was used to investigate the distribution of iron in rat organs and its localisation in liver subcellular fraction. A 57Fe-sucrose complex solution was injected by 0.5 ml doses into tail veins of animals every day, during a 6-day period.