INVOLVEMENT OF THE COPPER IN THE INHIBITION OF CU,ZN SUPEROXIDE-DISMUTASE ACTIVITY AT HIGH PH

被引:4
作者
CALABRESE, L
POLTICELLI, F
CAPO, C
MUSCI, G
机构
[1] UNIV ROME LA SAPIENZA,DEPT BIOCHEM SCI,PIAZZALE A MORO 5,I-00185 ROME,ITALY
[2] UNIV ROME LA SAPIENZA,CNR,CTR MOLEC BIOL,I-00185 ROME,ITALY
来源
FREE RADICAL RESEARCH COMMUNICATIONS | 1991年 / 12-3卷
关键词
D O I
10.3109/10715769109145799
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The alkaline spectroscopic transition of the copper at the active site of Cu, Zn superoxide dismutase has been reexamined by room temperature EPR. in order to correlate it with the inhibition of the enzyme activity at high pH. The EPR transition is governed by a single prototropic equilibrium, with pK values of 11.3 and 11.1 for ox and shark superoxide dismutase. respectively. This result suggests possible contributions of changes of the copper environment to the higher pK of the activity/pH curve. When Arg141 was cheniically modified by phenylglyoxal treatment of the ox protein. a lower pK value (10.8) was obtained, indicating that Arg141 is involved in the observed modifications of the EPR spectra. © 1991 Informa UK Ltd All rights reserved: reproduction in whole or part not permitted.
引用
收藏
页码:305 / 312
页数:8
相关论文
共 22 条
[1]   ELECTROSTATIC CONTROL OF THE RATE-DETERMINING STEP OF THE COPPER, ZINC SUPEROXIDE-DISMUTASE CATALYTIC REACTION [J].
ARGESE, E ;
VIGLINO, P ;
ROTILIO, G ;
SCARPA, M ;
RIGO, A .
BIOCHEMISTRY, 1987, 26 (11) :3224-3228
[2]   REDUCED ANION-BINDING AFFINITY OF CU,ZN SUPEROXIDE DISMUTASES CHEMICALLY MODIFIED AT ARGININE [J].
BERMINGHAMMCDONOGH, O ;
DEFREITAS, DM ;
KUMAMOTO, A ;
SAUNDERS, JE ;
BLECH, DM ;
BORDERS, CL ;
VALENTINE, JS .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1982, 108 (04) :1376-1382
[3]   INVESTIGATION OF CU2CO2SOD AND ITS ANION DERIVATIVES - NMR AND ELECTRONIC-SPECTRA [J].
BERTINI, I ;
LANINI, G ;
LUCHINAT, C ;
MESSORI, L ;
MONNANNI, R ;
SCOZZAFAVA, A .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1985, 107 (15) :4391-4396
[4]   PROPERTIES OF THE CUPRIC SITES IN BOVINE SUPEROXIDE-DISMUTASE STUDIED BY NUCLEAR-MAGNETIC-RELAXATION MEASUREMENTS [J].
BODEN, N ;
HOLMES, MC ;
KNOWLES, PF .
BIOCHEMICAL JOURNAL, 1979, 177 (01) :303-309
[5]   A COMPARISON OF THE EFFECTS OF CYANIDE, HYDROGEN-PEROXIDE, AND PHENYLGLYOXAL ON EUKARYOTIC AND PROCARYOTIC CU,ZN SUPEROXIDE DISMUTASES [J].
BORDERS, CL ;
FRIDOVICH, I .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1985, 241 (02) :472-476
[6]   SUBSTITUTION OF ARGININE FOR LYSINE 134 ALTERS ELECTROSTATIC PARAMETERS OF THE ACTIVE-SITE IN SHARK CU,ZN SUPEROXIDE-DISMUTASE [J].
CALABRESE, L ;
POLTICELLI, F ;
ONEILL, P ;
GALTIERI, A ;
BARRA, D ;
SCHININA, E ;
BOSSA, F .
FEBS LETTERS, 1989, 250 (01) :49-52
[7]  
CALABRESE L, 1983, OXY RADICALS THEIR S, V2, P179
[8]  
CUDD A, 1982, J BIOL CHEM, V257, P1443
[9]   CONSERVATION OF LOCAL ELECTRIC-FIELDS IN THE EVOLUTION OF CU,ZN SUPEROXIDE-DISMUTASE [J].
DESIDERI, A ;
FALCONI, M ;
PARISI, V ;
ROTILIO, G .
FEBS LETTERS, 1989, 250 (01) :45-48
[10]   MECHANISM OF ACTION OF SUPEROXIDE-DISMUTASE FROM PULSE-RADIOLYSIS AND ELECTRON-PARAMAGNETIC RESONANCE - EVIDENCE THAT ONLY HALF ACTIVE-SITES FUNCTION IN CATALYSIS [J].
FIELDEN, EM ;
ROBERTS, PB ;
BRAY, RC ;
LOWE, DJ ;
MAUTNER, GN ;
ROTILIO, G ;
CALABRESE, L .
BIOCHEMICAL JOURNAL, 1974, 139 (01) :49-60