Iron proteins redox properties

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. 

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... 

An unusual [2Fe-2S] ferredoxin with unique spectroscopic properties exists in association with cytochromes b and c, and is involved in respiratory electron transport in mitochondria, chloroplasts and certain bacteria. When isolated, the complex contains two b hemes, one c, heme and the 2Fe-2S protein. The 2Fe-2S protein from the bct complex (Sections 62.1.5.2.3 and 62.1.5.2.5) was purified from bovine mitochondria by Rieske et al.,162 and is referred to as the Rieske iron-sulfur protein. The properties of this protein have been reviewed763 and its topography in mitochondrial ubiquinol-cytochrome c reductase has been described.764 They have high redox potentials in the range+150-330 mV. 

Evidence is now accumulating to show that reactions involving metals might be the common denominator underlying AD and PD. In these disorders, an abnormal reaction between a protein and a redox-active metal ion (copper or iron) promotes the formation of ROS. It is especially intriguing how the antioxidant Cu/Zn-SOD activity can convert into a pro-oxidant activity, a theme echoed in the recent proposal that Ap and PrP, the proteins respectively involved in AD and prion diseases, possess similar redox properties [Bush, 2002],... 

Aconitase was the first protein to be identified as containing a catalytic iron-sulfur cluster [24-26]. It was also readily established that the redox properties of the [4Fe-4S](2+ 1+) cluster do not play a role of significance in biological functioning the 1 + oxidation state has some 30% of the activity of the 2+ state [25], Since then several other enzymes have been identified or proposed to be nonredox iron-sulfur catalysts. They are listed in Table 2. It appears that all are involved in stereospecific hydration reactions. However, these proteins are considerably less well characterized than aconitase. In particular, no crystal structural information is available yet. Therefore, later we summarize structural and mechanistic information on aconitase, noting that many of the basic principles are expected to be relevant to the other enzymes of Table 2. 

The extent of CPO immobilized on the sol-gel was determined by the difference between the activity of the initial enzyme solution and that measured in cumulative washes. Based on the cumulative activity lost in six washes, a second preparation of the CPO-bound sol-gel contained 10, 24, and 55 mg of CPO/g of sol-gel for the 50-, 150-, and 200-A CPO sol-gels, respectively. In prior experiments, the total activity was measured and an estimated 80% of the bound CPO was active. The sol-gel immobilization is expected to limit the unfolding of the protein bound inside pores of the sol-gel. Thus, immobilization is expected to affect solvent stability and thermostability. Immobilization would probably not impact peroxide stability, since the mechanism of peroxide inactivation is associated with changes in the redox properties and oxidation state of the heme iron and the active center, which cannot be protected by immobilization. Experimental studies of immobilized CPO were therefore limited to temperature and solvent stability. 

Therefore, it appears that the redox properties of the metallo-porphyrin are required only for the initiation step in these free-radical autoxidations and that the porphyrin is not a stoichiometrically significant catalyst (21, 22, 23). The failure of these simple approaches to a reaction iron-porphine oxide or its equivalent could indicate that the ligation state of iron in the protein, presumably including an axial thiolate, is crucial to the oxygen-transfer properties of P 450. Support... 

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