COPPER-ZINC SUPEROXIDE-DISMUTASE - A UNIQUE BIOLOGICAL LIGAND FOR BIOINORGANIC STUDIES

被引：77

作者：

VALENTINE, JS ^{[1
]}

DEFREITAS, DM ^{[1
]}

机构：

[1] LOYOLA UNIV,CHICAGO,IL 60626

来源：

JOURNAL OF CHEMICAL EDUCATION | 1985年 / 62卷 / 11期

关键词：

D O I：

10.1021/ed062p990

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

引用

页码：990 / 997

页数：8

共 28 条

[1] REDUCED ANION-BINDING AFFINITY OF CU,ZN SUPEROXIDE DISMUTASES CHEMICALLY MODIFIED AT ARGININE
BERMINGHAMMCDONOGH, O
DEFREITAS, DM
KUMAMOTO, A
SAUNDERS, JE
BLECH, DM
BORDERS, CL
VALENTINE, JS
[J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1982, 108 (04) : 1376 - 1382
[2] NOVEL CO(II) BINDING-SITE IN COPPER-FREE SUPEROXIDE-DISMUTASE - EVIDENCE FOR BINDING OF COBALT AT THE COPPER-BINDING SITE
CALABRESE, L
COCCO, D
DESIDERI, A
[J]. FEBS LETTERS, 1979, 106 (01) : 142 - 144
[3] COBALT BOVINE SUPEROXIDE-DISMUTASE - REACTIVITY OF COBALT CHROMOPHORE IN COPPER-CONTAINING AND IN COPPER-FREE ENZYME
CALABRESE, L
COCCO, D
MORPURGO, L
MONDOVI, B
ROTILIO, G
[J]. EUROPEAN JOURNAL OF BIOCHEMISTRY, 1976, 64 (02): : 465 - 470
[4] CARRICO RJ, 1970, J BIOL CHEM, V245, P723
[5] EXCHANGE OF HISTIDINE C-2 PROTONS IN SUPEROXIDE DISMUTASES - NOVEL METHOD FOR ASSIGNING HISTIDINE METAL LIGANDS IN PROTEINS
CASS, AEG
HILL, HAO
BANNISTER, JV
BANNISTER, WH
HASEMANN, V
JOHANSEN, JT
[J]. BIOCHEMICAL JOURNAL, 1979, 183 (01) : 127 - 132
[6] REDUCED ANION BINDING AND ANION INHIBITION IN CU,ZN SUPEROXIDE-DISMUTASE CHEMICALLY MODIFIED AT LYSINES WITHOUT ALTERATION OF THE RHOMBIC DISTORTION OF THE COPPER SITE
COCCO, D
MAVELLI, I
ROSSI, L
ROTILIO, G
[J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1983, 111 (03) : 860 - 864
[7] PHOSPHATE IS AN INHIBITOR OF COPPER-ZINC SUPEROXIDE-DISMUTASE
DEFREITAS, DM
VALENTINE, JS
[J]. BIOCHEMISTRY, 1984, 23 (09) : 2079 - 2082
[8] FEE JA, 1981, J BIOL CHEM, V256, P1910
[9] IS SUPEROXIDE IMPORTANT IN OXYGEN POISONING
FEE, JA
[J]. TRENDS IN BIOCHEMICAL SCIENCES, 1982, 7 (03) : 84 - 86
[10] BIOLOGY OF OXYGEN RADICALS
FRIDOVICH, I
[J]. SCIENCE, 1978, 201 (4359) : 875 - 880

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