Sulfur and Selenium: The Role of Oxidation State in Protein Structure and Function

Angewandte Chemie - International Edition - Tập 42 Số 39 - Trang 4742-4758 - 2003
Norbert Latruffe1, Gregory I. Giles2, Niroshini M. Giles2, Helmut Sies3
1School of Chemistry University of Exeter, Stocker Road, Exeter EX4 4QD, UK
2School of Chemistry, University of Exeter, Stocker Road, Exeter EX4 4QD, UK, Fax: (+44) 1392‐26‐3434
3Institute for Biochemistry and Molecular Biology I, Heinrich-Heine-Universität Düsseldorf, Postfach 101 007, 40 001, Düsseldorf, Germany

Tóm tắt

AbstractSulfur and selenium occur in proteins as constituents of the amino acids cysteine, methionine, selenocysteine, and selenomethionine. Recent research underscores that these amino acids are truly exceptional. Their redox activity under physiological conditions allows an amazing variety of posttranslational protein modifications, metal free redox pathways, and unusual chalcogen redox states that increasingly attract the attention of biological chemists. Unlike any other amino acid, the “redox chameleon” cysteine can participate in several distinct redox pathways, including exchange and radical reactions, as well as atom‐, electron‐, and hydride‐transfer reactions. It occurs in various oxidation states in the human body, each of which exhibits distinctive chemical properties (e.g. redox activity, metal binding) and biological activity. The position of selenium in the periodic table between the metals and the nonmetals makes selenoproteins ideal catalysts for many biological redox transformations. It is therefore apparent that the chalcogen amino acids cysteine, methionine, selenocysteine, and selenomethionine exhibit a unique biological chemistry that is the source of exciting research opportunities.

Từ khóa


Tài liệu tham khảo

2002, Thiol Metabolism and Redox Regulation of Cellular Functions, 1

2003, Cellular Implications of Redox Signalling

2000, Antioxidant and Redox Regulation of Genes, 1

2002, Protein Sensors and Reactive Oxygen Species, Part A: Selenoproteins and Thioredoxin, 1

2002, Protein Sensors and Reactive Oxygen Species, Part B: Thiol Enzymes and Proteins, 1

Torchinsky Y.M, 1981, Sulfur in Proteins, 1

Jocelyn P. C., 1972, Biochemistry of the SH Group

1988, Glutathione Conjugation: Mechanisms and Biological Significance, 1

10.1021/jo00055a016

10.1016/S0021-9258(18)34713-6

10.1007/978-1-4684-3282-4_1

10.1016/S0891-5849(99)00177-X

10.1016/S0891-5849(01)00480-4

10.1179/135100001101536427

Holmgren A., 1995, Struct. Bonding (Berlin), 3, 239

10.1016/B978-0-12-642760-8.50015-6

10.1146/annurev.bi.54.070185.001513

10.1142/9781848160033_0007

10.1515/BC.2002.042

10.1006/abbi.1994.1167

10.1016/S0065-230X(08)60848-9

10.1016/0006-2952(96)00142-6

10.1016/0006-291X(79)92009-6

10.1124/dmd.30.10.1053

10.1124/mol.63.1.136

10.1073/pnas.94.8.3621

10.1016/S0021-9258(18)33050-3

10.1021/bi9926431

10.1042/bj3460001

Spence J. T., 1988, Biochem. J., 250, 921, 10.1042/bj2500921

10.1021/tx980223r

10.1073/pnas.122061399

10.1146/annurev.biochem.71.110601.135406

10.1021/bi961007p

10.1126/science.287.5453.655

10.1021/ja029338e

10.1074/jbc.273.47.31016

10.1074/jbc.271.12.6827

10.1074/jbc.272.39.24216

10.1146/annurev.biochem.70.1.121

10.1146/annurev.biochem.70.1.209

10.1021/bi00015a032

10.1016/S0065-3233(01)58006-7

10.1021/bi00021a010

10.1021/bi00002a007

10.1021/bi9803630

10.1515/BC.2002.040

10.1073/pnas.96.22.12333

Schröder E., 2000, Struct. Bonding (Berlin), 8, 605

10.1016/B978-0-12-642760-8.50005-3

10.1002/ange.19860981203

10.1002/anie.198610581

Sies H., 2000, Encyclopedia of Stress, Vol. III, 102

10.1016/S0891-5849(01)00710-9

Giles G. I., 2002, Gen. Physiol. Biophys., 21, 65

10.1042/bj20011882

10.1074/jbc.M102417200

10.1074/jbc.M008260200

Nöhammer G., 2002, Thiol Metabolism and Redox regulation of Cellular Functions, 48

10.1016/0006-291X(86)90437-7

10.1016/0009-2797(89)90069-0

10.1096/fasebj.11.6.9194521

10.1006/abbi.2001.2368

10.1107/S090744499701216X

10.1073/pnas.171320998

10.1073/pnas.96.16.8884

10.1073/pnas.212640899

10.1016/0003-9861(83)90592-1

10.1016/0891-5849(94)00158-G

10.1016/S0047-6374(98)00152-3

10.1007/BF02003229

10.1073/pnas.93.26.15036

10.1021/bi0020269

10.1074/jbc.M006137200

10.1016/S0014-5793(00)01669-0

10.1073/pnas.91.1.237

10.1016/S0014-5793(99)01562-8

10.1073/pnas.95.7.3489

10.1073/pnas.96.5.1910

10.1080/02603598908035801

10.1006/bbrc.1998.9026

10.1073/pnas.95.7.3478

10.1089/15230860152542907

10.1016/S0014-5793(02)03890-5

10.1073/pnas.96.5.1936

10.1074/jbc.272.47.29454

10.1093/oxfordjournals.jbchem.a002976

10.1110/ps.9.5.1024

10.1006/bbrc.2001.5897

D. N. Kachru S. Khandelwal S. K. Tandon Biomed. Environ. Sci.1989 2 265–270.

10.1385/BTER:76:1:19

10.1007/s002040050279

10.1016/0022-2836(89)90498-1

10.1016/S0014-5793(01)03272-0

10.1007/BF01888363

10.1515/BC.2000.017

Brocklehurst K., 1998, Comprehensive Biological Catalysis, Vol. 2, 381

10.1021/bi00717a019

Eklund H., 1982, J. Biol. Chem., 257, 14 349, 10.1016/S0021-9258(19)45387-8

10.1016/S0009-2797(00)00263-5

10.1096/fasebj.12.12.1075

10.1038/37995

10.1016/S0140-6736(00)02490-9

10.1111/j.1749-6632.2000.tb06203.x

10.1039/B205802M

10.1016/S1382-6689(01)00078-3

10.1042/BJ20021853

10.1074/jbc.M300755200

Thanbichler M., 2002, Methods Enzymol., 347

10.1016/0003-9861(67)90136-1

10.1515/bchm3.1995.376.11.651

P. Mauri L. Benazzi L. Flohé M. Maiorino P. G. Pietta S. Pilawa A. Roveri F. Ursini Biol. Chem.2003 384 in press.

10.1515/BC.2000.107

10.1002/biof.5520110122

10.1080/10715760000300371

10.1006/abbi.1997.0462

10.1006/abbi.1999.1435

10.1016/0006-2952(84)90083-2

10.1021/tx990156g

10.1016/S0006-2952(97)00542-X

10.1039/b107972g

10.1021/cr000426w

10.1016/S0303-7207(99)00040-4

10.1016/S0076-6879(02)47014-0

10.1073/pnas.91.16.7708

Raaijmakers H., 2002, Struct. Bonding (Berlin), 10, 1261

10.1111/j.1574-6968.1988.tb02748.x

10.1021/ja0169163

10.1126/science.1073339

10.1093/emboj/cdf566

10.1517/13543784.9.3.607

10.1073/pnas.171178698

10.1074/jbc.272.49.30780

10.1515/bchm.1997.378.8.827

10.1074/jbc.M112115200

10.1021/bi00077a018

10.1046/j.1365-2958.2002.02851.x

Thông tin
Thông tin xuất bản

Angewandte Chemie - International Edition

Tập 42 Số 39

4742-4758

Thông tin tác giả