PREFERENTIAL PHOTOINACTIVATION OF CATALASE AND PHOTOINHIBITION OF PHOTOSYSTEM-II ARE COMMON EARLY SYMPTOMS UNDER VARIOUS OSMOTIC AND CHEMICAL STRESS CONDITIONS

被引:60
作者
STREB, P [1 ]
MICHAELKNAUF, A [1 ]
FEIERABEND, J [1 ]
机构
[1] JW GOETHE UNIV,INST BOT,POSTFACH 111932,D-60054 FRANKFURT,GERMANY
关键词
CATALASE; DCMU; FLUORESCENCE (VARIABLE; FV); GLUTATHIONE REDUCTASE; GLYCOLATE OXIDASE; HEAVY METALS; PARAQUAT; PEROXIDASE; PHOTOINHIBITION; PHOTOOXIDATION; PHOTOSYSTEM-II (D1-PROTEIN); RYE; SECALE-CEREALE;
D O I
10.1111/j.1399-3054.1993.tb01376.x
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Activity of catalase (EC 1.11.1.6) and variable fluorescence (F(v)) were measured in sections of rye leaves (Secale cereale L. cv. Halo) that were exposed for 24 h to moderately high irradiance under osmotic or chemical stress conditions (paraquat, DCMU, mannitol, NaCl, CdCl2, CuSO4, Pb(NO3)2, KNO2, or K2SO3. Changes of the chlorophyll content and of enzyme activities related to peroxide metabolism, such as glycolate oxidase, glutathione reductase, and peroxidase, were assayed for comparison. In the presence of the herbicides paraquat and low DCMU concentrations that exert only partial inhibition of photosynthesis, as well as after most treatments with osmotic or chemical stress factors, catalase markedly declined due to a preferential photoinactivation. At higher DCMU levels catalase did not decline. At low KNO2 concentrations catalase activity was preferentially increased. In general, photoinactivation of catalase was accompanied by a decline of the F(v)/F(m) ratio, indicating photoinhibition of photosystem II, while other parameters were much more stable. Inasmuch as both catalase and the D1 reaction center protein of photosystem II have a rapid turnover in light, their steady state levels appear to decline whenever stress effects either excessively enhance deleterious oxidative conditions and degradation (e. g. paraquat, low DCMU), or inhibit repair synthesis. Photoinactivation of catalase and of photosystem II represent specific and widely occurring early symptoms of incipient photodamage indicating stress conditions where the repair capacity is not sufficient. During prolonged exposures, e.g. to NaCl and CuSO4, chlorophyll was bleached in light and the rate of its photodegradation increased in proportion as the catalase level had declined. The results suggest that the enhanced susceptibility of leaf tissues to photooxidative damage which is widely observed in stressed plants is related to the early loss of catalase.
引用
收藏
页码:590 / 598
页数:9
相关论文
共 42 条
[1]   COPPER ENZYMES IN ISOLATED CHLOROPLASTS - POLYPHENOLOXIDASE IN BETA-VULGARIS [J].
ARNON, DI .
PLANT PHYSIOLOGY, 1949, 24 (01) :1-15
[2]   LETHAL HYDROXYL RADICAL PRODUCTION IN PARAQUAT-TREATED PLANTS [J].
BABBS, CF ;
PHAM, JA ;
COOLBAUGH, RC .
PLANT PHYSIOLOGY, 1989, 90 (04) :1267-1270
[3]   TOO MUCH OF A GOOD THING - LIGHT CAN BE BAD FOR PHOTOSYNTHESIS [J].
BARBER, J ;
ANDERSSON, B .
TRENDS IN BIOCHEMICAL SCIENCES, 1992, 17 (02) :61-66
[4]   PHOTOINACTIVATION OF CATALASES FROM MAMMAL LIVER, PLANT LEAVES AND BACTERIA . COMPARISON OF INACTIVATION CROSS SECTIONS AND QUANTUM YIELDS AT 406-NM [J].
BJORN, LO .
PHOTOCHEMISTRY AND PHOTOBIOLOGY, 1969, 10 (02) :125-&
[5]   PHOTOINACTIVATION OF CATALASE [J].
CHENG, L ;
KELLOGG, EW ;
PACKER, L .
PHOTOCHEMISTRY AND PHOTOBIOLOGY, 1981, 34 (01) :125-129
[6]   INHIBITION OF PHOTOSYSTEM-II PRECEDES THYLAKOID MEMBRANE LIPID-PEROXIDATION IN BISULFITE-TREATED LEAVES OF PHASEOLUS-VULGARIS [J].
COVELLO, PS ;
CHANG, A ;
DUMBROFF, EB ;
THOMPSON, JE .
PLANT PHYSIOLOGY, 1989, 90 (04) :1492-1497
[7]   MODE OF ACTION OF BIPYRIDYLIUM HERBICIDES, PARAQUAT AND DIQUAT [J].
DODGE, AD .
ENDEAVOUR, 1971, 30 (111) :130-&
[8]  
ELSTNER EF, 1991, FREE RADICAL RES COM, V12-3, P795
[9]   PHOTOINACTIVATION OF CATALASE OCCURS UNDER BOTH HIGH-TEMPERATURE AND LOW-TEMPERATURE STRESS CONDITIONS AND ACCOMPANIES PHOTOINHIBITION OF PHOTOSYSTEM-II [J].
FEIERABEND, J ;
SCHAAN, C ;
HERTWIG, B .
PLANT PHYSIOLOGY, 1992, 100 (03) :1554-1561
[10]   PHOTOINACTIVATION OF CATALASE INVITRO AND IN LEAVES [J].
FEIERABEND, J ;
ENGEL, S .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1986, 251 (02) :567-576