Chemistry Reference
In-Depth Information
translocation was observed in the reaction of
O
•−
with Tyr. Overall, there is
progress in the identification and quantitative determination of amino acid
residue products in their reaction with ROS in a complex biological environ-
ment, but further investigation is desired. The advancement of analytical tech-
niques will help unravel many new oxidized products in future studies to
understand the contribution of ROS in aging and diseases. Finally, product
studies in combination with the ROS-specific detection method will enhance
knowledge of the use of ROS by biological systems. This would not only
require very low detection of ROS in biological matrices at nanomolar levels
but it should also have high selectivity against ROS species such as
O
•−
,
1
O
2
,
and
•
OH.
REFERENCES
1 Sugamura, K. and Keaney, J.F., Jr. Reactive oxygen species in cardiovascular
disease.
Free Radic. Biol. Med.
2011,
51
, 978-992.
2 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.
3 Rains, J.L. and Jain, S.K. Oxidative stress, insulin signaling, and diabetes.
Free
Radic. Biol. Med.
2011,
50
, 567-575.
4 Rodacka, A., Serafin, E., and Puchala, M. Efficiency of superoxide anions in the
inactivation of selected dehydrogenases.
Radiat. Phys. Chem.
2010,
79
, 960-965.
5 Stadtman, E.R. Protein oxidation and aging.
Free Radic. Res.
2006,
40
, 1250-
1258.
6 Pattison, D.I., Rahmanto, A.S., and Davies, D.I. Photo-oxidation of proteins.
Pho-
tochem. Photobiol. Sci.
2012,
11
, 38-53.
7 Dalsgaard, T.K., Nielsen, J.H., Brown, B.E., Stadler, N., and Davies, M.J. Dityro-
sine, 3,4-Dihydroxyphenylalanine (DOPA), and radical formation from tyrosine
residues on milk proteins with globular and flexible structures as a result of
riboflavin-mediated photo-oxidation.
J. Agric. Food Chem.
2011,
59
, 7939-7947.
8 Stadtman, E.R. Free radical-mediated oxidation of proteins. In
Free Radical
Technology
, D.B. Wallace, ed. Taylor and Francis, Washington, 1997, pp. 71-78.
9 Schuessler, H. and Schilling, K. Oxygen effect in the radiolysis of proteins. Part
2. Bovine serum albumin.
Int. J. Radiat. Biol.
1984,
45
, 267-281.
10 Swallow, A.J. Effect of ionization radiation on proteins, RcO groups, peptide
bond cleavage, inactivation, -SH oxidation. In
Radiation Chemistry of Organic
Compounds
, A.J. Swallow, ed. Pergamon Press, New york, 1960, pp. 211-224.
11 Kopoldová, J. and Liebster, J. The mechanism of the radiation chemical degrada-
tion of amino acids-V. Radiolysis of norleucine, leucine and isoleucine in aqueous
solution.
Int. J. Appl. Radiat. Isot.
1963,
14
, 493-494, IN3-IN8, 495-498.
12 garrison, W.M. Reaction mechanisms in the radiolysis of peptides, polypeptides,
and proteins.
Chem. Rev.
1987,
87
, 381-398.
13 Davies, M.J. Reactive species formed on proteins exposed to singlet oxygen.
Photochem. Photobiol.
2004,
3
, 17-25.
Search WWH ::
Custom Search