Cluster redox potential, determination

Figure 1. Principle of the determination of short-lived cluster redox potential by kinetics methods. The reference electron donor, S of a given potential and the metal atoms are generated by a single puke. During cluster coalescence, the redox potential of the couple E°(M -Mn) progressively increases, so that an effective transfer is observed after a critical time when the cluster potential becomes higher than that of the reference, constituting a threshold. Repeatedly, a new adsorption of excess cations, M, onto the reduced cluster, (n xkch (dlows another electron transfer from S with incrementation of nuclearity. The subcritical clusters Mn(n

The redox potentials of short-lived silver clusters have been determined through kinetics methods using reference systems. Depending on their nuclearity, the clusters change behavior from electron donor to electron acceptor, the threshold being controlled by the reference system potential. Bielectronic systems are often used as electron donors in chemistry. When the process is controlled by critical conditions as for clusters, the successive steps of monoelectronic transfer (and not the overall potential), of which only one determines the threshold of autocatalytical electron transfer (or of development) must be separately considered. The present results provide the nuclearity dependence of the silver cluster redox potential in solution close to the transition between the mesoscopic phase and the bulk metal-like phase. A comparison with other literature data allows emphasis on the influence of strong interaction of the environment (surfactant, ligand, or support) on the cluster redox potential and kinetics. Rela-... 

Figure 5. Principle of the determination of short-lived cluster redox potential by kinetics method. The reference electron donor S of given potential and the metal atoms are generated by the same single pulse. Earing the cluster...

The same pifa,ox values as for the water-soluhle Rieske protein have been determined for the Rieske protein in bovine heart mitochondrial bci complex (102) this is consistent with the fact that the redox potential of the Rieske cluster is unperturbed within the bci complex and indicates that the environment of the Rieske cluster must be accessible within the complex. However, in the bci complex from Para-coccus denitrificans, the redox potential at pH 6.0 was found to be 45 mV lower than at pH 7, indicating the presence of a third group with a redox-dependent pi a value below 7 (36). No redox potential difference between pH 6 and 7 was found for the water-soluble Rieske... 

While the redox potentials of Rieske clusters are above -1-100 mV at pH 7, values between 100 and 150 mV have been determined for the redox potentials of Rieske-type clusters (Table XI). Several 4-cysteine coordinated [2Fe-2S] clusters have redox potentials similar to those of Rieske-type clusters, for example, the [2Fe-2S] clusters of the dioxygenase reductases [compilation in (104)]-, therefore, the redox potential is not useful for distinguishing between Rieske-type and ferredoxin-type clusters. 

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,... 

As described above, the combination of EPR and Mossbauer spectroscopies, when applied to carefully prepared parallel samples, enables a detailed characterization of all the redox states of the clusters present in the enzyme. Once the characteristic spectroscopic properties of each cluster are identified, the determination of their midpoint redox potentials is an easy task. Plots of relative amounts of each species (or some characteristic intensive property) as a function of the potential can be fitted to Nernst equations. In the case of the D. gigas hydrogenase it was determined that those midpoint redox potentials (at pFi 7.0) were —70 mV for the [3Fe-4S] [3Fe-4S]° and —290 and —340mV for each of the [4Fe-4S]> [4Fe-4S] transitions. 

For clusters of higher nuclearity too, the kinetic method for determining the redox potential °(M]] /M ) is based on electron transfer, for example, from mild reductants of known potential which are used as reference systems, towards charged clusters M](. [31] Note that the redox potential differs from the microelectrode potential M /M ) by the... 

Iron-sulfur proteins belong to the class of electron-transport proteins [29]. They contain an iron sulfur cluster, e.g. [4Fe-4S], which shuttles between different oxidation states. The structure of the cluster is quite consistent among a series of these proteins, but their redox potentials vary widely. Synthetic models of iron-sulfur proteins have been designed [30] to investigate the factors that determine the reduction potential of the core and to mimic other biologically... 

Ceruloplasmin is involved in copper storage and transport as well as in iron mobilisation and oxidation. Among the blue oxidases it is unique since it contains, in addition to the usual motif of a type 1 combined with the trinuclear cluster, two other type 1 coppers. Electron transfer occurs, however, only between five of the six copper ions since one of the type 1 centres is not catalytically relevant due to its too high redox potential. The redox potentials of the centres were determined and possible electron transfer pathways among the copper sites were discussed.101... 

The potentials determined for reduction of the Fe,S clusters indicate that they are not directly responsible for all of the changes in the EPR spectrum that have been associated with Ni. Furthermore, because three electrons appear to be involved in the redox chemistry associated with... 

By changing the reference potential in a series of redox monitors, it is then possible to determine the dependence of the cluster potential on the nuclearity. The general trend of increasing redox potential with nuclearity is the same for all metals in solution as it is illustrated in Fig. 2 in the case of E°(AgVAg,) q. However, in gas phase, the variation of the ionization potential IV(Ag ) exhibits the opposite trend versus the nuclearity n. Indeed, since the Fermi potential of the normal hydrogen electrode (NHE) in water is 4.5 eV, and since the solvation free energy of Ag decreases with size as deduced from the Born model, one can explain the two opposite variations with size of F°(Ag /AgJ q and IP (AgJ as illustrated in Fig. 2. 

Mitochondrial cytochrome c is perhaps the most widely studied of all metalloproteins with respect to its electrochemical properties. It is located in the inner-membrane space of mitochondria and transfers electrons between membrane-bound complex III and complex IV. The active site is an iron porphyrin with a redox potential (7) of -1-260 mV vs. NHE. The crystal structures of cytochrome c from tuna have been determined (8, 9) in both oxidation states at atomic resolution. It is found that the heme group is covalently linked to the protein via two thioether bridges, and part of its edge is exposed at the protein surface. Cytochrome c is a very basic protein, with an overall charge of -1-7/-l-8 at neutral pH. Furthermore, many of the excess basic lysine residues are clustered around the mouth of the heme crevice, giving rise to a pronounced charge asymmetry. 

An obvious application of direct electrochemistry of proteins is the determination of redox potentials. In cases of thermodynamically inaccessible or kinetically reactive species for which traditional potentio-metric methods are inappropriate, direct electrochemistry offers an alternative approach. A good example is the 7Fe ferredoxin from Azo-tobacter chroococcum, which contains one [4Fe-4S] and one [3Fe-4S] cluster. The [4Fe-4S] + potential obtained (7i) by cyclic voltamme-... 

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