Pathways of Oxidative Damage

Annual Review of Microbiology - Tập 57 Số 1 - Trang 395-418 - 2003
James A. Imlay1
1Department of Microbiology, University of Illinois, Urbana, Illinois 61801, USA. [email protected]

Tóm tắt

▪ Abstract  The phenomenon of oxygen toxicity is universal, but only recently have we begun to understand its basis in molecular terms. Redox enzymes are notoriously nonspecific, transferring electrons to any good acceptor with which they make electronic contact. This poses a problem for aerobic organisms, since molecular oxygen is small enough to penetrate all but the most shielded active sites of redox enzymes. Adventitious electron transfers to oxygen create superoxide and hydrogen peroxide, which are partially reduced species that can oxidize biomolecules with which oxygen itself reacts poorly. This review attempts to present our still-incomplete understanding of how reactive oxygen species are formed inside cells and the mechanisms by which they damage specific target molecules. The vulnerability of cells to oxidation lies at the root of obligate anaerobiosis, spontaneous mutagenesis, and the use of oxidative stress as a biological weapon.

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Tài liệu tham khảo

Abbe K, 1982, J. Bacteriol., 152, 175, 10.1128/jb.152.1.175-182.1982

10.1073/pnas.96.18.10412

10.1073/pnas.96.11.6161

Beauchamp C, 1970, J. Biol. Chem., 245, 5214, 10.1016/S0021-9258(18)62842-X

10.1006/abbi.1997.0343

10.1074/jbc.274.7.4202

10.1074/jbc.271.35.21037

Benov LT, 1994, J. Biol. Chem., 269, 25310, 10.1016/S0021-9258(18)47248-1

Bielski BHJ, 1983, J. Biol. Chem., 258, 4759, 10.1016/S0021-9258(18)32488-8

10.1063/1.555739

10.1021/ja00451a028

10.1038/262418a0

Briviba K, 1997, Biol. Chem., 378, 1259

10.1016/0378-1097(96)84203-0

10.1002/j.1460-2075.1986.tb04256.x

Chang EC, 1991, J. Biol. Chem., 266, 4417, 10.1016/S0021-9258(20)64338-1

10.1021/bi00011a008

10.1016/0167-4889(85)90156-9

10.1021/bi973035t

10.1016/0003-9861(91)90366-Q

10.1016/0891-5849(92)90042-F

10.1073/pnas.100422497

10.1128/JB.184.14.3774-3784.2002

10.1073/pnas.96.13.7502

10.1073/pnas.83.21.8268

10.1016/0968-0004(82)90151-7

Flint DH, Emptage MH. 1990. Dihydroxy-acid dehydratase: isolation, characterization as Fe-S proteins, and sensitivity to inactivation by oxygen radicals. InBiosynthesis of Branched Chain Amino Acids, ed. DCZ Barak, JV Schloss, pp. 285–314. New York: VCH

Flint DH, 1993, J. Biol. Chem., 268, 25547, 10.1016/S0021-9258(19)74426-3

Flint DH, 1993, J. Biol. Chem., 268, 22369, 10.1016/S0021-9258(18)41538-4

10.1016/0003-9861(91)90270-S

Gardner PR, 1991, J. Biol. Chem., 266, 19328, 10.1016/S0021-9258(18)55001-8

Gardner PR, 1992, J. Biol. Chem., 267, 8757, 10.1016/S0021-9258(19)50343-X

10.1016/S1367-5931(02)00364-2

10.1074/jbc.270.23.13681

10.1128/jb.179.2.382-388.1997

10.1046/j.1365-2958.1999.01343.x

Gort AS, 1998, J. Bacteriol., 180, 1402, 10.1128/JB.180.6.1402-1410.1998

10.1021/bi025599p

10.1074/jbc.M203089200

10.1006/abbi.1995.1068

10.1042/0264-6021:3530411

10.1046/j.1432-1327.2000.01809.x

10.1046/j.1432-1327.1999.00748.x

10.1016/S0005-2728(00)00252-8

Hille R, 1981, J. Biol. Chem., 256, 9090, 10.1016/S0021-9258(19)52512-1

Hutchinson F, 1985, Prog. Nucleic Acid Res., 32, 116

10.1046/j.1365-2958.2001.02638.x

10.1074/jbc.M206186200

Imlay JA, 1995, J. Biol. Chem., 270, 19767, 10.1016/S0021-9258(18)94548-5

Imlay JA, 1991, J. Biol. Chem., 266, 6957, 10.1016/S0021-9258(20)89596-9

10.1126/science.3287616

10.1126/science.2834821

10.1073/pnas.93.24.13635

10.1074/jbc.272.44.27652

10.1099/13500872-141-9-2271

Kuo CF, 1987, J. Biol. Chem., 262, 4724, 10.1016/S0021-9258(18)61255-4

10.1021/bi00125a014

10.1006/abbi.1993.1159

10.1016/0891-5849(94)90239-9

Mai X, 1994, J. Biol. Chem., 269, 16726, 10.1016/S0021-9258(19)89451-6

10.1128/jb.178.20.5890-5896.1996

Massey V, 1994, J. Biol. Chem., 36, 22459, 10.1016/S0021-9258(17)31664-2

10.1016/0006-291X(69)90287-3

McCord JM, 1969, J. Biol. Chem., 244, 6049, 10.1016/S0021-9258(18)63504-5

10.1073/pnas.68.5.1024

10.1074/jbc.274.15.10119

10.1074/jbc.M204958200

10.1016/S0006-291X(88)81075-1

10.1074/jbc.270.11.5812

10.1074/jbc.M005536200

10.1046/j.1365-2958.2001.02343.x

10.1128/JB.185.6.1942-1950.2003

10.1016/0167-4838(95)00029-T

10.1126/science.288.5471.1651

10.1006/jmbi.2001.5010

Rocha ER, 1999, J. Bacteriol., 181, 5701, 10.1128/JB.181.18.5701-5710.1999

10.1016/0014-5793(82)80388-8

10.1016/0014-5793(90)80651-X

10.1046/j.1365-2958.1998.00941.x

10.1021/ar00072a005

10.1128/JB.183.24.7173-7181.2001

10.1128/JB.183.24.7182-7189.2001

10.1006/abbi.1993.1019

10.1074/jbc.M004239200

10.1177/00220345850640110601

10.1111/j.1399-302X.1991.tb00497.x

10.1111/j.1432-1033.1996.0427u.x

10.1128/jb.177.9.2305-2314.1995

10.1073/pnas.83.11.3820

10.1128/JB.185.1.221-230.2003

10.1021/ar50088a003

10.1042/bj1820625

10.1016/S0891-5849(99)00051-9

10.1074/jbc.M203977200

10.1016/S0891-5849(01)00824-3