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Fe molecules

Fe(II) oxidized O2 consumed Fe/Molecule Buffer Analysis Reference... [Pg.190]

Figure 3. Comparison of the rate of oxidation of Fe(II) when mixed with apoferritin coats (480 Fe/molecule) in 0.15 M Hepes Na, pH 7.0, using absorbance at 420 nm ( a—s— ), availability to react with -phenanthroline ( o—o—o ), change in the x-ray absorption near edge structure (XANES) ( — — ). All three types of measurements were made under the same experimental conditions, including the sample holder. (Data are taken from Ref. Figure 3. Comparison of the rate of oxidation of Fe(II) when mixed with apoferritin coats (480 Fe/molecule) in 0.15 M Hepes Na, pH 7.0, using absorbance at 420 nm ( a—s— ), availability to react with -phenanthroline ( o—o—o ), change in the x-ray absorption near edge structure (XANES) ( — — ). All three types of measurements were made under the same experimental conditions, including the sample holder. (Data are taken from Ref.
Within aerobic biology, the harvesting of the oxidative energy of O2 is fundamental to oxidative metabohsm. Because this is accomplished via the electron-transfer oxidation of four cytochrome c(Fe ) molecules ( pH , +0.3 V vs. NHE) per O2, the challenge is to facilitate the reduction of O2 via four one-electron steps, each with a potential greater than +0.4 V versus NHE at pH 7 (equation 125). The thermodynamics for the uncatalyzed electron-transfer reduction of O2 does not meet this criterion (equation 126) especially for the initial pH-independent electron transfer to O2. [Pg.3479]

Fig 3. The 4,1 K Mbssbauer spectra of horse spleen apoferritin loaded with iron at pH 6,4 as follows (A) with four Fe/molecule, (B) with four Fe/molecule after preloading with 150 Fe, Iron was added as Fe(II) in air and samples were frozen 3 min later. (A> The relaxation subspectrum, a, is due to solitary Fe(III) atoms (B) the magnetic sextet, e, is due to large Fe(III) clusters. Both samples show a central doublet due to small Fe(III) clusters and in B there is a second unresolved doublet due to Fellll) dimers. All the added iron is Fe(III) at 3 min. At 90 K the sextet, e, of spectrum B, collapses into a doublet, but the subspectrum, a, of spectrum A, is also seen at this temperature. Reproduced from Ref 69. [Pg.459]

Table 12-1 Reductive Fe release from recombinant ferritins reconstituted to constant mineral size (480 Fe/molecule) the effect of proline substitution for the highly conserved leucine 134. Table 12-1 Reductive Fe release from recombinant ferritins reconstituted to constant mineral size (480 Fe/molecule) the effect of proline substitution for the highly conserved leucine 134.
Proceeding from the analysis of AFM images of the surface and profile sections of the adsorptive protecting layer (Figs. 2.49a and b, a conclusion has been made that Tet-Fe molecules form clusters of with a characteristic size of 250 x 300 nm in the 3-5 nm plane across the layer thickness on the metal surface [136]. [Pg.150]

FIGURE 7.1. Schematic illustration of the responses of liquid and solid surfaces to stress (a) a stressed hquid surface with vacancies (fe) molecules below the surface rapidly flow into the stressed area to heal the imbalance of forces (c) a stressed solid surface with various defects (d) due to lack of mobility, molecules cannot readily move into the stressed areas and the defects remain to produce a higher surface energy. [Pg.126]

C7H6O5. Colourless crystals with one molecule of water, m.p. 253" C, sparingly soluble in water and alcohol. It occurs free in woody tissue, in gall-nuts and in tea, and is a constituent of the tannins, from which it can be obtained by fermentation or by acid hydrolysis. It gives a blue-black colour with Fe and is used in the manufacture 6f inks. On heating it gives pyrogallol. [Pg.185]

Ti, B, Ni, Cr, Fe, Co, Mn) has been described, as was the synthesis of nonsiliceous materials such as oxides of W, Fe, Pb, Mo, and Sb [18]. Although these materials do not represent tme zeolites, they are highly interesting materials which are commonly covered in the zeolite literature with great potential for shape-selective catalysis of bulky molecules. [Pg.2782]

The excess chemiccil potential is thus determined from the average of exp[—lT (r )/fe In ensembles other than the canonical ensemble the expressions for the excess chem potential are slightly different. The ghost particle does not remain in the system and the system is unaffected by the procedure. To achieve statistically significant results m Widom insertion moves may be required. However, practical difficulties are encounte when applying the Widom insertion method to dense fluids and/or to systems contain molecules, because the proportion of insertions that give rise to low values of y f, dramatically. This is because it is difficult to find a hole of the appropriate size and sha... [Pg.459]

This is the point group to which all regular octahedral molecules, such as SFe (Figure 4.12b) and [Fe(CN)6], belong. [Pg.85]

Prussian Blue. Reaction of [Fe(CN)3] with an excess of aqueous h on(Ill) produces the finely divided, intensely blue precipitate Pmssian Blue [1403843-8] (tetrairon(Ill) tris(hexakiscyanoferrate)), Fe4[Fe(CN)3]. Pmssian Blue is identical to Turnbull s Blue, the name which originally was given to the material produced by reaction of [Fe(CN)3] with excess aqueous h on(Il). The soHd contains or has absorbed on its surface a large and variable number of water molecules, potassium ions (if present in the reaction), and h on(Ill) oxide. The h on(Il) centers are low spin and diamagnetic h on(Ill) centers are high spin. Variations of composition and properties result from variations in reaction conditions. Rapid precipitation in the presence of potassium ion affords a colloidal suspension of Pmssian Blue [25869-98-1] which has the approximate composition KFe[Fe(CN)3]. Pmssian Blue compounds are used as pigments in inks and paints and its formation on sensitized paper is utilized in the production of blueprints. [Pg.435]

The stmcture of Pmssian Blue and its analogues consists of a three-dimensional polymeric network of Fe —CN—Fe linkages. Single-crystal x-ray and neutron diffraction studies of insoluble Pmssian Blue estabUsh that the stmcture is based on a rock salt-like face-centered cubic (fee) arrangement with Fe centers occupying one type of site and [Fe(CN)3] units randomly occupying three-quarters of the complementary sites (5). The cyanides bridge the two types of sites. The vacant [Fe(CN)3] sites are occupied by some of the water molecules. Other waters are zeoHtic, ie, interstitial, and occupy the centers of octants of the unit cell. The stmcture contains three different iron coordination environments, Fe C, Fe N, and Fe N4(H20), in a 3 1 3 ratio. [Pg.435]

Substrate reduction is accompHshed by a series of sequential associations and dissociations of the two proteias, and duting each cycle, two molecules of MgATP are hydroly2ed and a single electron is transferred from the Fe proteia to the MoFe proteia (11,133), with the dissociation step being rate-limiting at about 6 (H)- Although the kinetics of aU. the partial reactions have been measured, Httie is known about the physical details of the... [Pg.88]

Gofactors. Frequendy proteins exist in their native state in association with other nonprotein molecules or cofactors, which are cmcial to their function. These may be simple metal ions, such as Fe " in hemerythrin or Ca " in calmodulin a heme group, as for the globins nucleotides, as for dehydrogenases, etc. [Pg.211]


See other pages where Fe molecules is mentioned: [Pg.387]    [Pg.187]    [Pg.190]    [Pg.314]    [Pg.6298]    [Pg.654]    [Pg.81]    [Pg.196]    [Pg.6297]    [Pg.64]    [Pg.520]    [Pg.387]    [Pg.187]    [Pg.190]    [Pg.314]    [Pg.6298]    [Pg.654]    [Pg.81]    [Pg.196]    [Pg.6297]    [Pg.64]    [Pg.520]    [Pg.107]    [Pg.124]    [Pg.257]    [Pg.356]    [Pg.56]    [Pg.687]    [Pg.604]    [Pg.946]    [Pg.2394]    [Pg.2697]    [Pg.2990]    [Pg.111]    [Pg.364]    [Pg.397]    [Pg.1148]    [Pg.209]    [Pg.40]    [Pg.40]    [Pg.439]    [Pg.441]    [Pg.384]    [Pg.130]    [Pg.233]   
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Are there alternative Fe(II) oxidation sites on ferritin molecules

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