A kinetic model for the regulation of electron transfer through the cyanide-resistant pathway in plant mitochondria

1993 ◽  
Vol 1142 (1-2) ◽  
pp. 165-174 ◽  
Author(s):  
James N. Siedow ◽  
Anthony L. Moore
2007 ◽  
Vol 129 (1) ◽  
pp. 225-232 ◽  
Author(s):  
András Szarka ◽  
Nele Horemans ◽  
Zita Kovács ◽  
Pál Gróf ◽  
Miklós Mayer ◽  
...  

2019 ◽  
Vol 215 ◽  
pp. 39-53 ◽  
Author(s):  
D. Buesen ◽  
T. Hoefer ◽  
H. Zhang ◽  
N. Plumeré

Redox-active films are advantageous matrices for the immobilization of photosynthetic proteins, due to their ability to mediate electron transfer as well as to achieve high catalyst loading on an electrode for efficient generation of electricity or solar fuels.


1976 ◽  
Vol 3 (2) ◽  
pp. 153 ◽  
Author(s):  
W.A Wickes ◽  
J.T Wiskish

The uncoupling by arsenate of beetroot and cauliflower bud mitochondria showed the following characteristics: (1) arsenate stimulation of respiration above the rate found with phosphate; (2) inhibition of arsenate-stimulated respiration by phosphate; (3) enhancement of arsenate-stimulated respiration by ADP; (4) only partial prevention of this ADP-enhanced respiration by atractyloside; (5) inhibition by oligomycin of the arsenate-stimulated respiration back to the phosphate rate; and (6) the absence of any stimulatory effect of ADP in the presence of oligomycin. These results are qualitatively analogous to those reported for arsenate uncoupling in rat liver mitochondria. Arsenate stimulated malate oxidation, presumably by stimulating malate entry, in both beetroot and cauliflower bud mitochondria; however, high rates of oxidation, and presumably entry, were only sustained with arsenate in beetroot mitochondria. NADH was oxidized rapidly in cauliflower bud mitochondria in the presence of arsenate, showing that arsenate did not inhibit electron transfer processes.


Sign in / Sign up

Export Citation Format

Share Document