REACTIVE SPECIES - Oxidation of Amino Acids, Peptides, and Proteins: Kinetics and Mechanism - page 30

peptides are described in Chapter 6. Unlike chromium and manganese, pro-
cesses using Fe(VI) are considered environmentally benign. Other oxidation
states of iron, ferrate(V) (Fe(V)) and ferrate(IV) (Fe(IV)), have shown much
higher reactivity than that of Fe(VI) and also have potential uses in oxidation
processes [300, 332-334]. Synthetic methods of ferrates are summarized in
Chapter 6. The reactivity of ferrates with molecules is highlighted for amino
acids and peptides (Chapter 6). The generation of Fe(V) species in the Fe(VI)-
TiO 2 -UV system has also been suggested as a method to degrade pollutants
and organisms [335]. The iron-tetraamidomacrocyclic ligand (Fe-TAML), a
catalyst in trace amounts, activates H 2 O 2 to produce reactive species, Fe IV =O
and Fe V =O, which oxidize numerous compounds of environmental interest
[336].
REFERENCES
1 Stadtman, E.R. Protein oxidation and aging. Free Radic. Res. 2006, 40 ,
1250-1258.
2 Winterbourn, C.C. Reconciling the chemistry and biology of reactive oxygen
species. Nature Chem. Biol. 2008, 4 , 278-286.
3 Murphy, M.P., Holmgren, A., Larsson, N.G., Halliwell, B., Chang, C.J., Kalyanara-
man, B., Rhee, S.G., Thornalley, P.J., Partridge, L., Gems, D., Nyström, T., Belousov,
V., Schumacker, P.T., and Winterbourn, C.C. Unraveling the biological roles of
reactive oxygen species. Cell Metab. 2011, 13 , 361-366.
4 Halliwell, B. The wanderings of a free radical. Free Radic. Biol. Med. 2009, 46 ,
531-542.
5 Baraibar, M.A., Hyzewicz, J., Rogowska-Wrzesinska, A., Ladouce, R., Roepstorff,
P., Mouly, V., and Friguet, B. Oxidative stress-induced proteome alterations target
different cellular pathways in human myoblasts. Free Radic. Biol. Med. 2011, 51 ,
1522-1532.
6 Spickett, C.M. and Pitt, A.R. Protein oxidation: role in signalling and detection
by mass spectrometry. Amino Acids 2012, 42 , 5-21.
7 Dickinson, B.C. and Chang, C.J. Chemistry and biology of reactive oxygen species
in signaling or stress responses. Nat. Chem. Biol. 2011, 7 , 504-511.
8 Mailloux, R.J. and Harper, M.E. Uncoupling proteins and the control of mito-
chondrial reactive oxygen species production. Free Radic. Biol. Med. 2011, 51 ,
1106-1115.
9 Gullotta, F., di Masi, A., Coletta, M., and Ascenzi, P. CO metabolism, sensing, and
signaling. Biofactors 2012, 38 , 1-13.
10 Little, J.W., Doyle, T., and Salvemini, D. Reactive nitroxidative species and noci-
ceptive processing: determining the roles for nitric oxide, superoxide, and per-
oxynitrite in pain. Amino Acids 2012, 42 , 75-94.
11 Salvemini, D., Little, J.W., Doyle, T., and Neumann, W.L. Roles of reactive oxygen
and nitrogen species in pain. Free Radic. Biol. Med. 2011, 51 , 951-966.
12 Davies, M.J. The oxidative environment and protein damage. Biochem. Biophys.
Acta—Proteins Proteomics 2005, 1703 , 93-109.