Biophysical Characterization of Mesophyll and Bundle Sheath Chloroplasts Isolated From the Leaves of Eleusine coracana, an Aspartate-Type C4 Plant. II. Photosynthetic Electron Transfer and Energy Conservation Reactions

1976 ◽  
Vol 3 (2) ◽  
pp. 185 ◽  
Author(s):  
CKM Rathnam ◽  
VSR Das

Mesophyll and bundle sheath chloroplasts isolated from the leaves of E. coracana, an aspartate-type C4 plant, have been utilized to study various photochemical activities in an effort to understand their high rates of photosysnthetic CO2 fixation. Bundle sheath chloroplasts were relatively more active in the overall process of photosynthetic electron transfer from water to NADP. Though photosystem II (PS II) and the associated non-cyclic photophosphorylation activities were of the same magnitude in both types of chloroplast, PS I and the associated cyclic photophosphorylation activities were three to four times more active in bundle sheath chloroplasts than in mesophyll chloroplasts. The influence of different illuminance on the electron and energy transfer reactions has been studied. At all the light levels tested, cyclic photophosphorylation activity was higher than non-cyclic in bundle sheath chloroplasts, while sigmoid kinetics were observed with mesophyll chloroplasts. Acid-base phosphorylation activities of the two types of chloroplast were similar. Heat treatment of the chloroplasts resulted in a selective inhibition of PS II in both types. Total leaf chlorophyll was approximately equally destributed between mesophyll and bundle sheath chloroplasts, which were found to have chlorophyll a-chlorophyll b ratios of 4.50 and 3.50 respectively. A working hypothesis for the energy requirements in the mesophyll and bundle sheath cells for the maintenance of various biochemical processes is proposed. It is also concluded that a greater part of the total leaf photochemical potential is associated with bundle sheath chloroplasts of E. coracana.

2005 ◽  
Vol 33 (4) ◽  
pp. 832-835 ◽  
Author(s):  
S.E. Hart ◽  
B.G. Schlarb-Ridley ◽  
D.S. Bendall ◽  
C.J. Howe

The respiratory chain of cyanobacteria appears to be branched rather than linear; furthermore, respiratory and photosynthetic electron-transfer chains co-exist in the thylakoid membrane and even share components. This review will focus on the three types of terminal respiratory oxidases identified so far on a genetic level in cyanobacteria: aa3-type cytochrome c oxidase, cytochrome bd-quinol oxidase and the alternative respiratory terminal oxidase. We summarize here their genetic, biochemical and biophysical characterization to date and discuss their interactions with electron donors as well as their physiological roles.


2001 ◽  
Vol 276 (33) ◽  
pp. 30598-30607 ◽  
Author(s):  
Javier G. Fernández-Velasco ◽  
Arash Jamshidi ◽  
Xiao-Song Gong ◽  
Jianhui Zhou ◽  
Rosie Y. Ueng

Author(s):  
Jörg Pieper ◽  
Leonid Rusevich ◽  
Thomas Hauß ◽  
Gernot Renger

AbstractThe effect of dehydration on the lamellar spacing of photosystem II (PS II) membrane fragments from spinach has been investigated using neutron membrane diffraction at room temperature. The diffraction data reveal a major peak at a scattering vector Q of 0.049 Å−1 at a relative humidity (r.h.) of 90% corresponding to a repeat distance D of about 129 Å. Upon dehydration to 44% r.h., this peak shifts to about 0.060 Å−1 corresponding to a distance of 104.7±2.5 Å. Within experimental error, the latter repeat distance remains almost the same at hydration levels below 44% r.h. indicating that most of the hydration water is removed. This result is consistent with the earlier finding that hydration-induced conformational protein motions in PS II membrane fragments are observed above 44% r.h. and correlated with the onset electron transfer in PS II (Pieper et al. 2008, Eur. Biophys. J. 37: 657–663).


Sign in / Sign up

Export Citation Format

Share Document