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Iron Sites

In the resting state, three water molecules occupy the coordination sites of the iron(II) that are located opposite to the three amino acid residues. Introduction of the a-ketoglutarate leads to displacement of two of the solvent molecules and [Pg.31]

3-dioxygenase from B. fuscum. All and dioxygen [56]. The identity of these bases is [Pg.35]


Wlien a strong electron-donor ligand such as pyridine is added to tlie reaction mixture, it can bond so strongly to tlie Rli tliat it essentially drains off all tlie Rli and shuts down tlie cycle it is called a catalyst poison. A poison for many catalysts is CO it works as a physiological poison in essentially the same way as it works as a catalyst poison it bonds to tlie iron sites of haemoglobin in competition witli O. ... [Pg.2703]

Iron Sulfur Compounds. Many molecular compounds (18—20) are known in which iron is tetrahedraHy coordinated by a combination of thiolate and sulfide donors. Of the 10 or more stmcturaHy characterized classes of Fe—S compounds, the four shown in Figure 1 are known to occur in proteins. The mononuclear iron site REPLACE occurs in the one-iron bacterial electron-transfer protein mbredoxin. The [2Fe—2S] (10) and [4Fe—4S] (12) cubane stmctures are found in the 2-, 4-, and 8-iron ferredoxins, which are also electron-transfer proteins. The [3Fe—4S] voided cubane stmcture (11) has been found in some ferredoxins and in the inactive form of aconitase, the enzyme which catalyzes the stereospecific hydration—rehydration of citrate to isocitrate in the Krebs cycle. In addition, enzymes are known that contain either other types of iron sulfur clusters or iron sulfur clusters that include other metals. Examples include nitrogenase, which reduces N2 to NH at a MoFe Sg homocitrate cluster carbon monoxide dehydrogenase, which assembles acetyl-coenzyme A (acetyl-CoA) at a FeNiS site and hydrogenases, which catalyze the reversible reduction of protons to hydrogen gas. [Pg.442]

What is the interaction between the Rieske-type cluster and the catalytic iron site of dioxygenases ... [Pg.151]

Fig. 6. A schematic view of the [3Fe-4S] Emd [4Fe-4S] cores, as versatile structures. The absence of one site leads to the formation of a [3Fe-4S] core. The cubane structure can incorporate different metals (in proteins, M = Fe, Co, Zn, Cd, Ni, Tl, Cs), and S, N, O may be coordinating atoms from hgands (Li). The versatihty csm be extended to higher coordination number at the iron site and a water molecule can even be a ligand, exchangeable with substrate (as in the case of aconitase (,87)). The most characteristic binding motifs are schematically indicated, for different situations proteins accommodating [3Fe-4S], [4Fe-4S], [3Fe-4S] + [4Fe-4S], and [4Fe-4S] -I- [4Fe-4S] clusters. A disulfide bridge may replace a cluster site (see text). Fig. 6. A schematic view of the [3Fe-4S] Emd [4Fe-4S] cores, as versatile structures. The absence of one site leads to the formation of a [3Fe-4S] core. The cubane structure can incorporate different metals (in proteins, M = Fe, Co, Zn, Cd, Ni, Tl, Cs), and S, N, O may be coordinating atoms from hgands (Li). The versatihty csm be extended to higher coordination number at the iron site and a water molecule can even be a ligand, exchangeable with substrate (as in the case of aconitase (,87)). The most characteristic binding motifs are schematically indicated, for different situations proteins accommodating [3Fe-4S], [4Fe-4S], [3Fe-4S] + [4Fe-4S], and [4Fe-4S] -I- [4Fe-4S] clusters. A disulfide bridge may replace a cluster site (see text).
The 3D crystal structure of Dsm. baculatum [NiSeFe] hydrogenase has been solved 185), and it was indicated that the enzyme contains three [4Fe-4S] centers. A cysteine (replacing a proline usually found near the [3Fe-4S] core) provides an extra ligand, enabling the acceptance of a fourth iron site at this cluster. [Pg.393]

The results of the XRD measurement showed that the Fe jAl, jPO catalyst was almost in amorphous state. Only a very broad peak at 29 of ca. 23 degree was observed. The Mossbauer spectroscopic study on this catalyst showed one doublet of iron with the isomeric shift of 0.31 mm s (a-Fe was used as the reference) and the quadrupole splitting of 0.62 mm s. These parameters are very close to those observed for FePO [13, 14], suggesting that the iron cation in the catalyst is tetrahedrally coordinated with oxygen and isolated by four PO tetrahedral units. Such coordination circumstance was suggested to be a key factor for the iron site effective for the oxidation of CH to CHjOH by H -Oj gas mixture [15]. [Pg.400]

Besides the absorption bands attributed to OH groups, another weak band at 1075 cm was observed at 473 K. This band can tentatively be assigned to an 0," species. The formation of Oj species with an absorption band at 1050-1200 cm was reported for many oxides [16-18]. Here, the 0, species must be formed on the reduced iron site through one electron transfer from Fe(II) to the adsorbed O,. However, this 0, species was very unstable because it... [Pg.401]

Very thick absorbers may be required for applied-field measurements to achieve reasonable absorption depths and measuring times because the Mossbauer spectra are usually split into several hyperfine components. Here the iron content may be as large as 100 pg Fe per cm (1.75 pmol Fe per cm ), which would correspond to t 1 for a two-line spectrum. For smdies of frozen solutions, Fe concentrations of 1 mM are desirable for each nonequivalent iron site [35]. [Pg.52]

In a conventional Fe Mossbauer experiment with a powder sample, one would observe a so-called quadrupole doublet with two resonance lines of equal intensities. The separation of the lines, as given by (4.36), represents the quadrupole splitting The parameter Afg is of immense importance for chemical applications of the Mossbauer effect. It provides information about bond properties and local symmetry of the iron site. Since the quadrupole interaction does not alter the mean energy of the nuclear ground and excited states, the isomer shift S can also be derived from the spectrum it is given by the shift of the center of the quadrupole spectrum from zero velocity. [Pg.93]

Fig. 8.18 Fe Mossbauer spectra of the trinuclear complex [Fe3(iptrz)6(H20)6](Trifl)6 recorded at the indicated temperatures. Only the central Fe(Il) site undergoes thermally induced ST, HScfred) LS (blue). The outer two Fe(II) sites, which remain in HS state at all temperatures, feel the ST occurring at the central iron site through a molecular distortion, the latter giving rise to a new quadrupole doublet, HSq HSo ° (from [35])... Fig. 8.18 Fe Mossbauer spectra of the trinuclear complex [Fe3(iptrz)6(H20)6](Trifl)6 recorded at the indicated temperatures. Only the central Fe(Il) site undergoes thermally induced ST, HScfred) LS (blue). The outer two Fe(II) sites, which remain in HS state at all temperatures, feel the ST occurring at the central iron site through a molecular distortion, the latter giving rise to a new quadrupole doublet, HSq HSo ° (from [35])...

See other pages where Iron Sites is mentioned: [Pg.729]    [Pg.2703]    [Pg.442]    [Pg.169]    [Pg.12]    [Pg.34]    [Pg.37]    [Pg.361]    [Pg.60]    [Pg.90]    [Pg.91]    [Pg.150]    [Pg.197]    [Pg.246]    [Pg.374]    [Pg.375]    [Pg.376]    [Pg.379]    [Pg.382]    [Pg.426]    [Pg.426]    [Pg.427]    [Pg.430]    [Pg.440]    [Pg.443]    [Pg.446]    [Pg.453]    [Pg.454]    [Pg.454]    [Pg.463]    [Pg.467]    [Pg.485]    [Pg.397]    [Pg.405]    [Pg.497]    [Pg.52]    [Pg.86]    [Pg.396]    [Pg.429]    [Pg.435]    [Pg.436]   


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