Relationship between the Hydrolysis of Adenosine Triphosphate and Oxidative Phosphorylation

Nature ◽  
1957 ◽  
Vol 180 (4582) ◽  
pp. 372-374 ◽  
Author(s):  
W. C. HÜLSMANN ◽  
E. C. SLATER
Keyword(s):  
Oxidative Phosphorylation ◽  
Adenosine Triphosphate ◽  
Hydrolysis Of

Hydrolysis of Adenosine Triphosphate by Trichloracetic Acid

Science ◽  
1949 ◽  
Vol 110 (2859) ◽  
pp. 402-402 ◽  
Author(s):  
A. Bernhard ◽  
L. Rosenbloom
Keyword(s):  
Adenosine Triphosphate ◽  
Trichloracetic Acid ◽  
Hydrolysis Of

The Coupling of Electron Transfer in Nitrogenase to the Hydrolysis of Magnesium Adenosine Triphosphate

1979 ◽  
Vol 7 (4) ◽  
pp. 633-636 ◽  
Author(s):  
ROGER N. F. THORNELEY ◽  
DAVID J. LOWE ◽  
ROBERT R. EDAY ◽  
RICHARD W. MILLER
Keyword(s):  
Electron Transfer ◽  
Adenosine Triphosphate ◽  
Hydrolysis Of

Equilibrium Constant of the Galactokinase Reaction and Free Energy of Hydrolysis of Adenosine Triphosphate

Nature ◽  
1959 ◽  
Vol 184 (4703) ◽  
pp. 1925-1927 ◽  
Author(s):  
M. R. ATKINSON ◽  
ELEANOR JCHNSON ◽  
R. K. MORTON
Keyword(s):  
Free Energy ◽  
Equilibrium Constant ◽  
Adenosine Triphosphate ◽  
Hydrolysis Of

Mitochondrial Complex I Function Affects Halothane Sensitivity in Caenorhabditis elegans 

2004 ◽  
Vol 101 (2) ◽  
pp. 365-372 ◽  
Author(s):  
Ernst-Bernhard Kayser ◽  
Phil G. Morgan ◽  
Margaret M. Sedensky
Keyword(s):  
Caenorhabditis Elegans ◽  
Oxidative Phosphorylation ◽  
Oxidative Damage ◽  
Adenosine Triphosphate ◽  
Complex I ◽  
Volatile Anesthetics ◽  
Mitochondrial Proteins ◽  
Wild Type ◽  
Complex Ii ◽  
C Elegans

Background : The gene gas-1 encodes a subunit of complex I of the mitochondrial electron transport chain in Caenorhabditis elegans. A mutation in gas-1 profoundly increases sensitivity of C. elegans to volatile anesthetics. It is unclear which aspects of mitochondrial function account for the hypersensitivity of the mutant. Methods : Oxidative phosphorylation was determined by measuring mitochondrial oxygen consumption using electron donors specific for either complex I or complex II. Adenosine triphosphate concentrations were determined by measuring luciferase activity. Oxidative damage to mitochondrial proteins was identified using specific antibodies. Results : Halothane inhibited oxidative phosphorylation in isolated wild-type mitochondria within a concentration range that immobilizes intact worms. At equal halothane concentrations, complex I activity but not complex II activity was lower in mitochondria from mutant (gas-1) animals than from wild-type (N2) animals. The halothane concentrations needed to immobilize 50% of N2 or gas-1 animals, respectively, did not reduce oxidative phosphorylation to identical rates in the two strains. In air, adenosine triphosphate concentrations were similar for N2 and gas-1 but were decreased in the presence of halothane only in gas-1 animals. Oxygen tension changed the sensitivity of both strains to halothane. When nematodes were raised in room air, oxidative damage to mitochondrial proteins was increased in the mutant animal compared with the wild type. Conclusions : Rates of oxidative phosphorylation and changes in adenosine triphosphate concentrations by themselves do not control anesthetic-induced immobility of wild-type C. elegans. However, they may contribute to the increased sensitivity to volatile anesthetics of the gas-1 mutant. Oxidative damage to proteins may be an important contributor to sensitivity to volatile anesthetics in C. elegans.

Sign in / Sign up

Export Citation Format

Share Document