Disease relevance of Spectroscopy, Mossbauer

• Using 57Fe Mössbauer spectroscopy of E. coli cells containing overexpressed FNR, we show here that the same cluster conversion also occurs in vivo on exposure to O2 [1].
• Resolution of multiple heme centers of hydroxylamine oxidoreductase from Nitrosomonas. 2. Mössbauer spectroscopy [2].
• Incubation with iron ions, cysteine and Synechocystis IscS led to the formation of one [2Fe2S] cluster at an IscA dimer as demonstrated (by the binding of about one iron and one sulfide ion per IscA monomer) by UV/Vis, EPR and Mössbauer spectroscopy [3].

High impact information on Spectroscopy, Mossbauer

• Mossbauer spectroscopy revealed the presence of a four cysteine-coordinated nonoxidizable [2Fe-2S]2+ cluster that bridges two Grx2 molecules via two structural Cys residues to form dimeric holo Grx2 [4].
• High-pressure Mössbauer spectroscopy on several compositions across the (Mg,Fe)O magnesiowüstite solid solution confirms that ferrous iron (Fe(2+)) undergoes a high-spin to low-spin transition at pressures and for compositions relevant to the bulk of the Earth's mantle [5].
• Using 57Fe or 56Fe for activation we have studied with Mössbauer spectroscopy the beef heart enzyme in the presence of citrate [6].
• Mössbauer spectroscopy of anaerobically purified HemN has identified a predominantly [4Fe-4S](2+) cluster in which only three iron atoms were coordinated by cysteine residues (isomer shift of delta = 0.43 (1) mm/s) [7].
• Mössbauer spectroscopy of whole cells at various states of (57)Fe-labeled chrysobactin uptake showed that this enzyme is not required for iron removal from chrysobactin in vivo [8].

Chemical compound and disease context of Spectroscopy, Mossbauer

• Escherichia coli iron enterobactin uptake monitored by Mössbauer spectroscopy [9].

Biological context of Spectroscopy, Mossbauer

• Diferric transferrin samples labelled with 57Fe at the N- or the C-terminal binding sites are compared by Mössbauer spectroscopy at 15 K and in zero magnetic field [10].

Anatomical context of Spectroscopy, Mossbauer

• Spin and valence states of the non-heme iron and the heme iron of cytochrome b559, as well as their interactions with alpha-tocopherol quinone (alpha-TQ) in photosystem II (PSII) thylakoid membranes prepared from the Chlamydomonas reinhardtii PSI- mutant have been studied using Mössbauer spectroscopy [11].
• Investigation of the interaction of triethyltin with rat liver mitochondria using binding studies and Mössbauer spectroscopy [12].
• Acetylphenylhydrazine induced haemoglobin oxidation in erythrocytes studied by Mössbauer spectroscopy [13].

Associations of Spectroscopy, Mossbauer with chemical compounds

• According to Mössbauer spectroscopy on purified FNR and cells containing overexpressed FNR, the [4Fe-4S]2+ cluster of FNR is converted by O2 to a [2Fe-2S]2+ in high yield [14].
• In this communication, results of revised sulfide analyses, iron-sulfur cluster displacement studies, and Mössbauer spectroscopy are presented that lead to the conclusion that the native enzyme contains a tetranuclear [4Fe-4S] center in a diamagnetic state [15].
• Mössbauer spectroscopy shows that purple aconitase has high-spin ferric ions, each residing in a tetrahedral environment of sulfur atoms [16].
• Mössbauer spectroscopy conclusively demonstrates that, under the commonly used assay conditions, dithiothreitol chelates ferrous ion and hence competes with the enzyme for binding the ferrous substrate [17].
• In this work we studied the spectroscopic and electrochemical properties of 4-HBCR by EPR and Mössbauer spectroscopy and identified the pterin cofactor as molybdopterin mononucleotide [18].

Gene context of Spectroscopy, Mossbauer

• The iron deficiencies of the ftnA and fur mutants were confirmed by Mössbauer spectroscopy, which further showed that the low iron contents of ftnA mutants are due to a lack of magnetically ordered ferric iron clusters likely to correspond to FtnA iron cores [19].
• Mössbauer spectroscopy of ferrous ion incubated with ferrochelatase in the absence of dithiothreitol shows a somewhat broad quadrupole doublet [17].
• We have studied beef heart cytochrome c oxidase at 4.2 K with Mössbauer spectroscopy using the 57Fe present in natural abundance [20].
• (Pyrz, J. W., Sage, J. T., Debrunner, P. G., and Que, Jr., L. (1986) J. Biol Chem. 261, 11015-11020) using Mossbauer spectroscopy and dithionite-reduced 57Fe-reconstituted uteroferrin [21].
• The previously reported S = 7/2 state of the enzyme during benzoyl-CoA-independent ATPase activity (Boll, M., Albracht, S. J. P., and Fuchs, G. (1997) Eur. J. Biochem. 244, 840-851) was confirmed by Mössbauer spectroscopy [22].

Analytical, diagnostic and therapeutic context of Spectroscopy, Mossbauer

• The valence of iron doped in the TiO(2), phase formation, defect structures, band gaps, and magnetic properties of the resultant nanopowders were systematically investigated using Mössbauer spectroscopy, XRD, Raman spectroscopy, TEM/HRTEM, UV-vis spectroscopy, and measurements of magnetic properties [23].
• An unusual discontinuity in the pressure derivatives of C11 and C12 at 4.7+/-0.2 GPa corresponds to the pressure at which the onset of a magnetic ordering transition is observed by high-pressure Mössbauer spectroscopy and neutron powder diffraction [24].
• Iron mobilization by deferoxamine from iron-loaded rat heart cells in culture was studied by electron microscopy and Mössbauer spectroscopy to identify the chelatable iron pool [25].

References