Clusters redox properties

Size Dependence of E (Ag, -Ag ). The quantum-size effect on metal clusters redox properties in solution is the most important feature for cluster chemistry in solution. Most of data have been obtained on silver clusters suitable as an experimental model (J-4, 22). 

It was emphasized that cluster redox properties depended on the nuclearity, mostly at low n values. The oligomers are spontaneously unstable with respect to coalescence and the determination of the redox properties of these transient oligomers is again accessible only by means of a kinetic approach. The clusters are formed as above by using a pulse to induce atoms which then coalesce during the coalescence they can react with an added reactant. Depending on the chemical properties of the reactant and on their nuclearity n, the clusters may behave as electron acceptors or donors. 

The second step involves the transfer of electrons from the reduced [FMNHg] to a series of Fe-S proteins, including both 2Fe-2S and 4Fe-4S clusters (see Figures 20.8 and 20.16). The unique redox properties of the flavin group of FMN are probably important here. NADH is a two-electron donor, whereas the Fe-S proteins are one-electron transfer agents. The flavin of FMN has three redox states—the oxidized, semiquinone, and reduced states. It can act as either a one-electron or a two-electron transfer agent and may serve as a critical link between NADH and the Fe-S proteins. 

The MoFe proteins exhibit complex redox properties. Each tetra-meric a2/32 molecule of MoFe protein contains two P clusters and two FeMoco centers and, as normally isolated in the presence of sodium dithionite, the FeMoco centers are EPR-active, exhibiting an S = spin state with g values near 4.3 and 3.7 and 2.01 (Fig. 6). The P clusters are EPR silent and there is a wealth of evidence (39) using a variety of techniques that indicates that the iron atoms in these clusters are all reduced to the Fe state. 

Cluster Attribution, Redox Properties, and Electron Exchange... 

The redox properties of a series of heterometal clusters were assessed by electrochemical and FPR measurements. The redox potentials of derivatives formed in D. gigas Fdll were measured by direct square wave voltammetry promoted by Mg(II) at a vitreous carbon electrode, and the following values were determined 495, 420,... 

Pierik, A.J., Wassink, H., Haaker, H., and Hagen, W.R. 1993. Redox properties and EPR spectroscopy of the P clusters of Azotobacter vinelandii MoFe protein. European Journal of Biochemistry 212 51-61. 

Metallothioneins (MT) are unique 7-kDa proteins containing 20 cysteine molecules bounded to seven zinc atoms, which form two clusters with bridging or terminal cysteine thiolates. A main function of MT is to serve as a source for the distribution of zinc in cells, and this function is connected with the MT redox activity, which is responsible for the regulation of binding and release of zinc. It has been shown that the release of zinc is stimulated by MT oxidation in the reaction with glutathione disulfide or other biological disulfides [334]. MT redox properties led to a suggestion that MT may possesses antioxidant activity. The mechanism of MT antioxidant activity is of a special interest in connection with the possible antioxidant effects of zinc. (Zinc can be substituted in MT by some other metals such as copper or cadmium, but Ca MT and Cu MT exhibit manly prooxidant activity.)... 

Diener MD, Bolskar RD, Alford JM (2002) Redox properties and purification of endohedral metallofullerenes. In Akasaka T, Nagase S (eds.) Endofullerenes a new family of carbon clusters. Kluwer, Dordrecht, pp. 133-151. 

Let us consider briefly but systematically the redox properties of a few homonuclear metal-sulfur clusters in order of increasing metal atom number. 

For the cytochrome c-plastocyanin complex, the kinetic effects of cross-linking are much more drastic while the rate of the intracomplex transfer is equal to 1000 s in the noncovalent complex where the iron-to-copper distance is expected to be about 18 A, it is estimated to be lower than 0.2 s in the corresponding covalent complex [155]. This result is all the more remarkable in that the spectroscopic and thermodynamic properties of the two redox centers appear weakly affected by the cross-linking process, and suggests that an essential segment of the electron transfer path has been lost in the covalent complex. Another system in which such conformational effects could be studied is the physiological complex between tetraheme cytochrome and ferredoxin I from Desulfovibrio desulfuricans Norway the spectral and redox properties of the hemes and of the iron-sulfur cluster are found essentially identical in the covalent and noncovalent complexes and an intracomplex transfer, whose rate has not yet been measured, takes place in the covalent species [156]. 

Pierik AJ, Hagen WR, Redeker JS, et al. 1992. Redox properties of the iron-snlfnr clusters in activated iron-hydrogenase from Desulfovibrio vulgaris (Hildenbor-ough). Eur J Biochem 209 63-72. 

A novel HZSM-5-supported N-interstitial Reio cluster catalyst has now exhibited the highest phenol selectivity (93.9%) using O2 as the sole oxidant at a good benzene conversion of 9.9% [107]. Although rhenium with various valences possesses oxophilic and redox properties similar to molybdenum and vanadium, it has not been widely used as catalyst for selective oxidation because of the easy sublimation of Re207. However, rhenium acts as a good component of oxidation catalysts under reductive atmosphere, for example, coexisting with methanol [108-110] and ammonia [111-114]. 

High-potential iron proteins, 45 313-314, 344 cluster stability, 45 324-332 function, 45 315-316 residues, 45 322-344 structure and, 45 317-322 redox properties, 45 333-344 solvent accessibility, 45 330, 332-333 source and function, 45 314-316 structure, 45 316-322 hydrogen bonding and, 45 321-322 intermolecular aggregation, 45 322 primary, 45 317-318 secondary and tertiary, 45 318-321... 

Stability means that clusters do not undergo coalescence nor corrosion by the medium, at least in the absence of oxygen. The quite negative value of ii°(MVM ) and the dependence of the cluster redox potential on the nuclearity have crucial consequences in the formation of early nuclei, their possible corrosion or their growth. As an example, the faster the coalescence, the lower is the probability of corrosion of the small clusters by the medium. The property of stability offers the means to apply to these clusters a larger amount of suitable characterization techniques than to transient oligomers. 

Fig. 10. Hypothetical reaction cycle for D. gigas hydrogenase, based on the EPR and redox properties of the nickel (Table II). Only the nickel center and one [4Fe-4S] cluster are shown. Step 1 enzyme, in the activated conformation and Ni(II) oxidation state, causes heterolytic cleavage of H2 to produce a Ni(II) hydride and a proton which might be associated with a ligand to the nickel or another base in the vicinity of the metal site. Step 2 intramolecular electron transfer to the iron-sulfur cluster produces a protonated Ni(I) site (giving the Ni-C signal). An alternative formulation of this species would be Ni(III) - H2. Step 3 reoxidation of the iron-sulfur cluster and release of a proton. Step 4 reoxidation of Ni and release of the other proton.

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