0000000000880799
AUTHOR
V. I. Goldanskii
Dynamics of protein-water systems revealed by Rayleigh scattering of Mössbauer radiation (RSMR)
A critical review of recent studies of protein dynamics by the RSMR technique is given. The main approximations in quantitative analyses of RSMR data are discussed and conclusions about dynamical properties of protein and interprotein water, deduced from experiments, are described.
Hemoglobin dynamics in rat erythrocytes investigated by M�ssbauer spectroscopy
Rats have been enriched in 57Fe and erythrocytes were isolated from the blood. Mössbauer absorption spectroscopy on the hemoglobin of these erythrocytes has shown rather similar dynamics as found earlier in crystals of myoglobin, in frozen solutions of human hemoglobin and in a number of other proteins. The results strongly indicate that the motion of the heme and presumably some part of the F-helix is mainly influenced by the average viscosity of the sample determined by a network of hydrogen bridges and other weak interactions. Extrapolations of Mössbauer results from protein crystals to proteins in their physiological surroundings seem to be suitable for heme proteins.
Mössbauer Spectroscopy on Photosynthetic Bacteria: Investigation of Reaction Centers of Rhodopseudomonas Viridis
Crystals of 57Fe enriched reaction centers have been investigated by Mossbauer spectroscopy. The cytochrome irons are in the low spin ferric state. The non-heme iron of the electron accepting side is partly ferrous high spin and partly ferrous low spin (or ferric high spin). Under the conditions of the experiment sodium ascorbate reduces only one cytochrome iron into the ferrous low spin state. Membrane bound proteins become flexible at higher temperatures than proteins with a hydrophilic surface. They are also less flexible, at least up to temperatures of about 250 K.
Mössbauer spectroscopy on the reaction center of Rhodopseudomonas viridis
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…
Temperature dependence of the dynamics of ultrafine particles in a polymeric network
Simple model systems with pronounced dynamical features will help to get a deeper insight into the complicated dynamics of large molecular networks. We investigated the bounded diffusion of ultrafine Fe(OH)3 particles (∼30 A in diameter) in the three-dimensional network of the cation exchanger Dowex 50 W which was solvated with a water solution of sucrose (60 wt%). Mossbauer spectra were recorded in the temperature range from 80 K to 305 K. At temperatures above 250 K broad diffusional lines of different widths appear in the spectrum proving the bounded nature of the diffusion. The line widths strongly increase with temperature to values of several hundred mm/s. Around 300 K a large portion…