In Situ Localization of Nadp-Malic Enzyme in Bundle Sheath Cells and Leaf Carbon Isotope Fractionation in Two C4Grasses

1996 ◽  
Vol 157 (1) ◽  
pp. 118-122 ◽  
Author(s):  
S. Madhavan ◽  
Carlos S. Andreo ◽  
Veronica G. Maurino ◽  
Marion H. O'Leary
Keyword(s):  
Carbon Isotope ◽  
Malic Enzyme ◽  
Isotope Fractionation ◽  
Bundle Sheath ◽  
Carbon Isotope Fractionation ◽  
Bundle Sheath Cells ◽  
Sheath Cells

Photosynthesis in Gomphrena celosioides and Its Classification Amongst C4-pathway Plants

1976 ◽  
Vol 3 (6) ◽  
pp. 863 ◽  
Author(s):  
E Repo ◽  
MD Hatch
Keyword(s):  
Malate Dehydrogenase ◽  
Malic Enzyme ◽  
Bundle Sheath ◽  
Mesophyll Cells ◽  
C4 Species ◽  
Bundle Sheath Cells ◽  
Major Route ◽  
Gomphrena Celosioides ◽  
A Minor ◽  
Sheath Cells

Monocotyledonous C4 species classified as NADP-ME-type transfer malate from mesophyll to bundle sheath cells where this acid is decarboxylated via NADP malic enzyme (EC 1.1.1.40) to yield pyruvate and CO2. The dicotyledon G. celosioides is most appropriately classified in thls group on the basis of high leaf activities of NADP malic enzyme and NADP malate dehydrogenase (EC 1.1.1.82). However, this species contains high aspartate aminotransferase (EC 2.6.1.1) and alanine aminotransferase (EC 2.6.1.2) activities and centripetally located bundle sheath chloroplasts, features more typical of other groups of C4 species that cycle aspartate and alanine between mesophyll and bundle sheath cells. During the present study, we found that these aminotransferases and NADP malate dehydrogenase were predominantly located in mesophyll cells, that malate was the major C4 acid labelled when leaves were exposed to 14CO2, and that label was initially lost most rapidly from the C-4 of malate during a chase in 12CO2. These results are consistent with the major route of photosynthetic metabolism being the same as that operative in other NADP-ME-type species, although this may be supplemented by a minor route utilizing aspartate. In contrast to monocotyledonous NADP-ME-type C4 species, isolated bundle sheath cells from G. celosioides were capable of rapid photoreduction of NADP as judged by products formed during assimilation of 14CO2 and their capacity for light-dependent oxygen evolution. This was related to a relatively high frequency of single unstacked granum in the chloroplasts of these cells.

Microbial in situ degradation of aromatic hydrocarbons in a contaminated aquifer monitored by carbon isotope fractionation

2003 ◽  
Vol 65 (1-2) ◽  
pp. 101-120 ◽  
Author(s):  
Hans H. Richnow ◽  
Eva Annweiler ◽  
Walter Michaelis ◽  
Rainer U. Meckenstock
Keyword(s):  
Carbon Isotope ◽  
Aromatic Hydrocarbons ◽  
Isotope Fractionation ◽  
Contaminated Aquifer ◽  
Carbon Isotope Fractionation ◽  
In Situ Degradation

Mitochondrial Respiration in Relation to Photosynthetic C4 Acid Decarboxylation in C4 Species

1996 ◽  
Vol 23 (1) ◽  
pp. 1 ◽  
Author(s):  
A Agostino ◽  
HW Heldt ◽  
MD Hatch
Keyword(s):  
Malic Enzyme ◽  
Type Species ◽  
Phosphoenolpyruvate Carboxykinase ◽  
Alternative Oxidase ◽  
Bundle Sheath ◽  
C4 Species ◽  
Bundle Sheath Cells ◽  
A Minor ◽  
Mitochondrial Malate Dehydrogenase ◽  
Sheath Cells

Certain respiratory features of bundle sheath cells isolated from the C4 species Urochloa panicoides (phosphoenolpyruvate carboxykinase (PCK)-type)), Panicum miliaceum (NAD malic enzyme (NAD-ME)-type) and Zea mays (NADP malic enzyme (NADP-ME)-type) were examined in relation to the requirements of the C4 acid decarboxylation step of C4 photosynthesis. Cells from both PCK-type and NAD-ME-type species showed high rates of malate-dependent respiration; with ADP or uncoupler the rates were in the range 2-3 μatom O min-1 mg-1 chlorophyll, about 5-10-times the rates with other respiratory substrates. Studies with inhibitors of cytochrome oxidase and the alternative oxidase indicated negligible alternative oxidase-mediated malate respiration in cells from Z. mays, a minor contribution in U. panicoides cells, but possibly a major role for this oxidase in the respiration of P. miliaceum cells. These differences were related to the different roles of respiration in photosynthetic C4 acid decarboxylation. Oxaloacetate strongly suppressed malate-dependent respiration in P. miliaceum bundle sheath cells but not in U. panicoides cells. This difference in the response to oxaloacetate was not due to different kinetic features of the mitochondrial malate dehydrogenase but was apparently largely due to the much lower activity of the enzyme in U. panicoides bundle sheath mitochondria. We propose that insensitivity of respiration to oxaloacetate in bundle sheath cells of PCK-type species may be essential for maintaining the C4 acid decarboxylation process. The reverse may be true for NAD-ME- type species.

Differential accumulation of plastid transcripts encoding photosystem II components in the mesophyll and bundle-sheath cells of monocotyledonous NADP-malic enzyme-type C4 plants

Planta ◽  
1991 ◽  
Vol 184 (3) ◽  
Author(s):  
Peter Westhoff ◽  
Karin Offermann-Steinhard ◽  
Michael H�fer ◽  
Kenneth Eskins ◽  
Angela Oswald ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Malic Enzyme ◽  
Bundle Sheath ◽  
C4 Plants ◽  
Bundle Sheath Cells ◽  
Sheath Cells

Subdivision of C4-Pathway Species Based on Differing C4 Acid Decarboxylating Systems and Ultrastructural Features

1975 ◽  
Vol 2 (2) ◽  
pp. 111 ◽  
Author(s):  
MD Hatch ◽  
T Kagawa ◽  
S Craig
Keyword(s):  
Malic Enzyme ◽  
Phosphoenolpyruvate Carboxykinase ◽  
Bundle Sheath ◽  
Intracellular Location ◽  
Bundle Sheath Cells ◽  
C4 Pathway ◽  
Malic Enzyme Activity ◽  
Mitochondrial Respiratory Enzyme ◽  
The Relationship ◽  
Sheath Cells

A selection of C4 species was surveyed to determine the relationship between their content of C4 acid decarboxylating enzymes, the activities of several other enzymes implicated in the C4 pathway, and their anatomical and ultrastructural features. The species examined clearly fell into three groups according to whether they contained high levels of either NADP malic enzyme (EC 1.1.1.40), phosphoenolpyruvate carboxykinase (EC 4.1.1.49) or NAD malic enzyme (EC 1.1 .1.39). The occurrence of high NADP malic enzyme activity was always associated with higher NADP malate dehydrogenase activity, while those species distinguished by high activities of either of the other two decarboxylases invariably contained high aspartate aminotransferase and alanine amino- transferase activities. Each of these decarboxylating enzymes was located in bundle sheath cells. NAD malic enzyme, but not phosphoenolpyruvate carboxykinase, was associated with mitochondria. Light and electron micrographs revealed differences between these groups with respect to the intracellular location of chloroplasts and mitochondria in bundle sheath cells, and the content and ultrastructure of mitochondria. The trend was for species with high NAD malic enzyme to contain the most mitochondria in the bundle sheath cells with apparently the most extensively developed cristae membrane systems. However, mitochondrial respiratory enzyme activities were similar for the three groups of species. The basic similarities and differences between the three groups of C4 plants distinguished by their differing C4 acid decarboxylating systems are discussed, and schemes for the probable photosynthetic reactions in bundle sheath cells are presented. A nomenclature to distinguish between these groups is proposed.

Monitoring in situ biodegradation of benzene and toluene by stable carbon isotope fractionation

2005 ◽  
Vol 24 (1) ◽  
pp. 51-60 ◽  
Author(s):  
Andrea Vieth ◽  
Matthias Kästner ◽  
Mario Schirmer ◽  
Holger Weiß ◽  
Stefan Gödeke ◽  
...  
Keyword(s):  
Carbon Isotope ◽  
Isotope Fractionation ◽  
Stable Carbon Isotope ◽  
Stable Carbon ◽  
Carbon Isotope Fractionation ◽  
Stable Carbon Isotope Fractionation ◽  
In Situ Biodegradation

Differential biogenesis of photosystem-II in mesophyll and bundle-sheath cells of 'malic' enzyme NADP+-type C4 plants. A comparative protein and RNA analysis

1990 ◽  
Vol 190 (1) ◽  
pp. 185-194 ◽  
Author(s):  
Angela OSWALD ◽  
Monika STREUBEL ◽  
Ulf LJUNGBERG ◽  
Jurgen HERMANS ◽  
K. ESKINS ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Malic Enzyme ◽  
Bundle Sheath ◽  
C4 Plants ◽  
Rna Analysis ◽  
Bundle Sheath Cells ◽  
Sheath Cells

Stable Carbon Isotope Fractionation during Enhanced In Situ Bioremediation of Trichloroethene

2002 ◽  
Vol 36 (10) ◽  
pp. 2262-2268 ◽  
Author(s):  
Donald L. Song ◽  
Mark E. Conrad ◽  
Kent S. Sorenson ◽  
Lisa Alvarez-Cohen
Keyword(s):  
Carbon Isotope ◽  
Isotope Fractionation ◽  
Stable Carbon Isotope ◽  
Stable Carbon ◽  
In Situ Bioremediation ◽  
Carbon Isotope Fractionation ◽  
Stable Carbon Isotope Fractionation

Aspartate Decarboxylation in Bundle Sheath Cells of Zea mays and Its Possible Contribution to C3 Photosynthesis

1981 ◽  
Vol 8 (2) ◽  
pp. 237 ◽  
Author(s):  
KSR Chapman ◽  
MD Hatch
Keyword(s):  
Zea Mays ◽  
Oxygen Evolution ◽  
Malic Enzyme ◽  
Bundle Sheath ◽  
Limited Capacity ◽  
C4 Species ◽  
Bundle Sheath Cells ◽  
C3 Photosynthesis ◽  
Mitochondrial Aspartate Aminotransferase ◽  
Sheath Cells

Strands of bundle sheath cells isolated from the NADP malic enzyme type C4 species, Zea mays, rapidly decarboxylate malate via NADP malic enzyme. The present studies show that these cells also decarboxylate aspartate, but at much lower rates. Aspartate decarboxylation is dependent upon added 2-oxoglutarate, is partially light dependent, and apparently proceeds via the following reaction sequence: aspartate ͛4 oxaloacetate ͛4 malate ͛4 pyruvate + CO2. Studies of the activity, properties, and location of enzymes indicated that these reactions are catalysed by a mitochondrial aspartate aminotransferase, mitochondrial or cytoplasmic NAD malate dehydrogenase, and chloroplast-located NADP malic enzyme, respectively. A mitochondria preparation isolated from Z. mays bundle sheath cells converted aspartate to oxaloacetate (with 2-oxoglutarate) and also pyruvate to alanine (with glutamate); the preparation did not reduce oxaloacetate to malate or decarboxylate malate at significant rates. Bundle sheath strands of Z. mays have a relatively limited capacity for HCO3- plus ribose 5-phosphate dependent oxygen evolution and rates were almost as high with aspartate plus 2-oxoglutarate. We suggest that amongst NADP malic enzyme type C4 species there may be a direct relationsip between the capacity of bundle sheath cells to decarboxylate aspartate and their potential for the photosystem II-mediated oxygen evolution.

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