Search results for "Metmyoglobin"
showing 7 items of 7 documents
Low temperature optical spectroscopy of low-spin ferric hemeproteins
1996
We report the Soret absorption spectra (500-350 nm) of the cyanomet derivatives of human hemoglobin and horse myoglobin, in the temperature range 300-20 K and in two different solvents (65% v/v glycerol-water or 65% v/v ethylene glycol-water). In order to obtain information on stereodynamic properties of active site of the two hemeproteins, we perform an analysis of the band profiles within the framework of electron-vibrations coupling. This approach enables us to single out the various contributions to the spectral bandwidth, such as those arising from non-radiative decay of the excited electronic state (homogeneous broadening) and from the coupling of the electronic transition i) with hig…
Structural factors controlling ligand binding to myoglobin: a kinetic hole-burning study.
1998
Using temperature-derivative spectroscopy in the temperature range below 100 K, we have studied the dependence of the Soret band on the recombination barrier in sperm whale carbonmonoxy myoglobin (MbCO) after photodissociation at 12 K. The spectra were separated into contributions from the photodissociated species, Mb*CO, and CO-bound myoglobin. The line shapes of the Soret bands of both photolyzed and liganded myoglobin were analyzed with a model that takes into account the homogeneous bandwidth, coupling of the electronic transition to vibrational modes, and static conformational heterogeneity. The analysis yields correlations between the activation enthalpy for rebinding and the model p…
An unambiguous procedure for discovering relaxation influence on M�ssbauer spectra
1994
A mathematical procedure which gives an opportunity to distinguish between relaxation and distribution mechanisms of the Mossbauer line broadening is proposed. It is based on the method of Mossbauer line sharpening developed recently [1] and allows one to answer unambiguously the question whether or not relaxation manifests itself in Mossbauer measurements by examining the wings of the spectrum. The procedure is applied to the spectra of high spin ferric metmyoglobin and (Fe0.65Ni0.35)1−xMnx alloys. Analysis of the metmyoglobin spectra manifests the presence of the relaxation influence in the temperature range 10 K≦T≦100 K. Analysis of the alloy spectra shows that for the temperatures 4 K≦T…
SAXS Study on Myoglobin Embedded in Amorphous Saccharide Matrices
2011
We report on Small Angle X-ray Scattering (SAXS) measurements performed on samples of carboxy-myoglobin and met-myoglobin embedded in low hydrated matrices of four different saccharides (trehalose, sucrose, maltose and lactose). Results confirm the already reported occurrence of inhomogeneities, which are not peculiar of trehalose samples, but appear also in maltose and lactose, and in some cases also sucrose, being dependent on the sample hydration and on the presence of sodium dithionite. This behaviour confirms our previous interpretation about the nature of the inhomogeneities, and prompt it as a possible general behaviour for highly concentrated sugar matrices.
Myoglobin on Silica: A Case Study of the Impact of Adsorption on Protein Structure and Dynamics
2013
International audience; If protein structure and function changes upon adsorption are well documented, modification of adsorbed protein dynamics remains a blind spot, despite its importance in biological processes. The adsorption of metmyoglobin on a silica surface was studied by isotherm measurements, microcalorimetry, circular dichroïsm, and UV-visible spectroscopy to determine the thermodynamic parameters of protein adsorption and consequent structure modifications. The mean square displacement and the vibrational densities of states of the adsorbed protein were measured by elastic and inelastic neutron scattering experiments. A decrease of protein flexibility and depletion in low freque…
X-ray structure determination of a metastable state of carbonmonoxy myoglobin after photodissociation.
1996
The x-ray structure of carbon monoxide (CO)-ligated myoglobin illuminated during data collection by a laser diode at the wavelength lambda = 690 nm has been determined to a resolution of 1.7 A at T = 36 K. For comparison, we also measured data sets of deoxymyoglobin and CO-ligated myoglobin. In the photon-induced structure the electron density associated with the CO ligand can be described by a tube extending from the iron into the heme pocket over more than 4 A. This density can be interpreted by two discrete positions of the CO molecule. One is close to the heme iron and can be identified to be bound CO. In the second, the CO is dissociated from the heme iron and lies on top of pyrrole ri…
Rayleigh scattering of Mössbauer radiation on a myoglobin single crystal
1992
The RSMR technique was used to determine the fraction of radiation which is scattered elastically and inelastically, respectively, into Bragg reflections of a metmyoglobin single crystal. From this measurement 〈x2 1c〉=0.027±0.008 A2 has been determined which is due to long range correlated motions in analogy to acoustic and optic modes in solids.