Ribulose-1,5-bisphosphate carboxylase/oxygenase content, assimilatory charge, and mesophyll conductance in leaves

被引:49
作者
Eichelmann, H [1 ]
Laisk, A [1 ]
机构
[1] Tartu Ulikooli Mol Rakubiol Inst, EE-51010 Tartu, Estonia
关键词
D O I
10.1104/pp.119.1.179
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
The content of ribulose-l,5-bisphosphate carboxylase/oxygenase (Rubisco) (E-t; EC 4.1.1.39) measured in different-aged leaves of sunflower (Helianthus annuus) and other plants grown under different light intensities, varied from 2 to 75 mu mol active sites m(-2) Mesophyll conductance (mu) was measured under 1.5% O-2, as well as postillumination CO2 uptake (assimilatory charge, a gas-exchange measure of the ribulose-1,5-bisphosphate pool). The dependence of mu on E-t saturated at E-t = 30 mu mol active sites m(-2) and mu = 11 mm s(-1) in high-light-grown leaves. In low-light-grown leaves the dependence tended toward saturation at similar E-t but reached a mu of only 6 to 8 mm s(-1). mu was proportional to the assimilatory charge, with the proportionality constant (specific carboxylation efficiency) between 0.04 and 0.075 mu M-1 s(-1). Our data show that the saturation of the relationship between E-t and mu is caused by three limiting components: (a) the physical diffusion resistance (a minor limitation), (b) less than full activation of Rubisco (related to Rubisco activase and the slower diffusibility of Rubisco at high protein concentrations in the stroma), and (c) chloroplast metabolites, especially S-phosphoglyceric acid and free inorganic phosphate, which control the reaction kinetics of ribulose-1,5-bisphosphate carboxylation by competitive binding to active sites.
引用
收藏
页码:179 / 189
页数:11
相关论文
共 63 条
[1]   INTERACTION OF SUGAR PHOSPHATES WITH THE CATALYTIC SITE OF RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE [J].
BADGER, MR ;
LORIMER, GH .
BIOCHEMISTRY, 1981, 20 (08) :2219-2225
[2]   THE RELATIONSHIP BETWEEN STEADY-STATE GAS-EXCHANGE OF BEAN-LEAVES AND THE LEVELS OF CARBON-REDUCTION-CYCLE INTERMEDIATES [J].
BADGER, MR ;
SHARKEY, TD ;
VONCAEMMERER, S .
PLANTA, 1984, 160 (04) :305-313
[3]   EFFECTS OF IRRADIANCE AND METHYL VIOLOGEN TREATMENT ON ATP, ADP, AND ACTIVATION OF RIBULOSE BISPHOSPHATE CARBOXYLASE IN SPINACH LEAVES [J].
BROOKS, A ;
PORTIS, AR ;
SHARKEY, TD .
PLANT PHYSIOLOGY, 1988, 88 (03) :850-853
[4]  
CAMPBELL WJ, 1992, PLANT CELL PHYSIOL, V33, P751
[5]   ELECTRON-TRANSPORT THROUGH PHOTOSYSTEM-I STIMULATES LIGHT ACTIVATION OF RIBULOSE BISPHOSPHATE CARBOXYLASE OXYGENASE (RUBISCO) BY RUBISCO ACTIVASE [J].
CAMPBELL, WJ ;
OGREN, WL .
PLANT PHYSIOLOGY, 1990, 94 (02) :479-484
[6]  
CRAFTSBRANDNER SJ, 1991, PLANTA, V183, P300, DOI 10.1007/BF00197802
[7]   LIGHT AND CO2 LIMITATION OF PHOTOSYNTHESIS AND STATES OF THE REACTIONS REGENERATING RIBULOSE 1,5-BISPHOSPHATE OR REDUCING 3-PHOSPHOGLYCERATE [J].
DIETZ, KJ ;
HEBER, U .
BIOCHIMICA ET BIOPHYSICA ACTA, 1986, 848 (03) :392-401
[8]   Physical and kinetic evidence for an association between sucrose-phosphate synthase and sucrose-phosphate phosphatase [J].
Echeverria, E ;
Salvucci, ME ;
Gonzalez, P ;
Paris, G ;
Salerno, G .
PLANT PHYSIOLOGY, 1997, 115 (01) :223-227
[9]   SLOW INACTIVATION OF RIBULOSEBISPHOSPHATE CARBOXYLASE DURING CATALYSIS IS CAUSED BY ACCUMULATION OF A SLOW, TIGHT-BINDING INHIBITOR AT THE CATALYTIC SITE [J].
EDMONDSON, DL ;
BADGER, MR ;
ANDREWS, TJ .
PLANT PHYSIOLOGY, 1990, 93 (04) :1390-1397
[10]   CO2 UPTAKE AND ELECTRON-TRANSPORT RATES IN WILD-TYPE AND A STARCHLESS MUTANT OF NICOTIANA-SYLVESTRIS - THE ROLE AND REGULATION OF STARCH SYNTHESIS AT SATURATING CO2 CONCENTRATIONS [J].
EICHELMANN, H ;
LAISK, A .
PLANT PHYSIOLOGY, 1994, 106 (02) :679-687