Proteins redox oxidation initiated

If a second redox protein is present under the conditions represented by Eq. 3 or 5, secondary protein-protein ET reactions can occur, again subject to thermodynamic and kinetic constraints. In this situation, however, the constraints can be modulated by having the higher potential (under oxidizing conditions) or lower potential (under reducing conditions) protein present in stoichiometric excess, thereby favoring removal of electrons from (or entry of electrons into) the appropriate protein in the initial reaction with exogenous flavin. 

Although in humans only MsrBl is a selenoprotein, the depletion of selenium from the diet of mice led to increases in both R and S stereoisomers. This was not initially explained, yet a subsequent study has shown that small molecule selenols (organic selenocysteine homologues) could act as efficient electron donors in vitro for MsrA enzymes. ° This effect has only been shown in vitro, but the possibility that small molecular selenium reductants, or more likely that some selenoproteins that contain reduced selenols (in redox-active motifs) is quite intriguing. Several small selenoproteins do not have real roles and reside in nearly all subcompartments of the cell (mitochondria, ER) where electron donors for Msr enzymes are probably critical to maintain protein stability. Low selenium nutritional status would then have a significant impact on all methionine oxidation, as Future studies to address selenium nutrition and methionine oxidation could prove to be... 

Mononuclear octahedral/trigonal bipyramidal iron centers are found in either the ferric or the ferrous oxidation state (Whittaker etal., 1984 Arciero et ai, 1983). Because the iron may participate directly in catalysis as either a Lewis acid or base, only one state is the active form for a given enzyme. Transient redox changes may occur during turnover, but the enzyme returns to its initial condition. In contrast the tetrahedral mononuclear iron proteins appear to function primarily as electron transfer agents and therefore change oxidation state with a single turnover. 

The superoxide oxide radical interacts with nitric oxide to produce peroxynitrite at a rate which three times faster than the rate at which superoxide dismutase utilizes superoxide (Beckman, 1994). Peroxynitrite is capable of diffusing to distant places in neural cells where it induces lipid peroxidation and may be involved in synaptosomal and myelin damage (Van der Veen and Roberts, 1999). After protonation and decomposition, peroxynitrite produces more hydroxyl radicals. This mechanism of hydroxyl radical generation is not dependent on redox active metal ions and may be involved in initiating lipid and protein peroxidation in vivo (Warner et al., 2004). 

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. 

The role of these interesting plasma membrane-dependent, vanadate-stimulated NAD(P)H oxidation reactions in cellular metabolism remains to be elucidated, although multiple interactions with cellular metabolism and components are possible including interactions with xanthine oxidase and lipid peroxidation [24], Decavanadate has been shown to enhance cytochrome c reduction [31], and cytochrome c release from mitochondria is associated with initiation of apoptosis. Perhaps the reduced cytochrome c is more readily released from the mitochondria. With increasing emphasis on the redox properties of vanadium being important in its pharmacological effects, it is quite possible that these reactions, either protein dependent or not, may play a role in therapeutic actions of vanadium. 

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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