scholarly journals Structure and Function of Cytochrome c Maturation Proteins

2007 ◽  
Vol 47 (2) ◽  
pp. 112-117
Author(s):  
Takeshi UCHIDA
Keyword(s):  
Cytochrome C ◽  
Structure And Function ◽  
Cytochrome C Maturation ◽  
And Function

ChemInform Abstract: Structure and Function of Cytochrome c Oxidase

ChemInform ◽  
2010 ◽  
Vol 22 (3) ◽  
pp. no-no ◽  
Author(s):  
F. MALATESTA ◽  
G. ANTONINI ◽  
P. SARTI ◽  
B. VALLONE ◽  
M. BRUNORI
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Structure And Function ◽  
Abstract Structure ◽  
And Function

The metal centers of cytochrome c oxidase: Structure and function

1983 ◽  
Vol 79 ◽  
pp. 72-73 ◽  
Author(s):  
Sunney I. Chan ◽  
David F. Blair ◽  
Craig T. Martin ◽  
Hsin Wang ◽  
Jeff Gelles ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Structure And Function ◽  
Metal Centers ◽  
And Function

Alteration of structure and function of ATP synthase and cytochrome c oxidase by lack of Fo-a and Cox3 subunits caused by mitochondrial DNA 9205delTA mutation

2015 ◽  
Vol 466 (3) ◽  
pp. 601-611 ◽  
Author(s):  
Kateřina Hejzlarová ◽  
Vilma Kaplanová ◽  
Hana Nůsková ◽  
Nikola Kovářová ◽  
Pavel Ješina ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Atp Synthase ◽  
Stop Codon ◽  
Threshold Effect ◽  
Structure And Function ◽  
Missense Mutations ◽  
Atp Production ◽  
Atp6 Gene ◽  
And Function

Mutations in the MT-ATP6 gene are frequent causes of severe mitochondrial disorders. Typically, these are missense mutations, but another type is represented by the 9205delTA microdeletion, which removes the stop codon of the MT-ATP6 gene and affects the cleavage site in the MT-ATP8/MT-ATP6/MT-CO3 polycistronic transcript. This interferes with the processing of mRNAs for the Atp6 (Fo-a) subunit of ATP synthase and the Cox3 subunit of cytochrome c oxidase (COX). Two cases described so far presented with strikingly different clinical phenotypes–mild transient lactic acidosis or fatal encephalopathy. To gain more insight into the pathogenic mechanism, we prepared 9205delTA cybrids with mutation load ranging between 52 and 99% and investigated changes in the structure and function of ATP synthase and the COX. We found that 9205delTA mutation strongly reduces the levels of both Fo-a and Cox3 proteins. Lack of Fo-a alters the structure but not the content of ATP synthase, which assembles into a labile, ∼60 kDa smaller, complex retaining ATP hydrolytic activity but which is unable to synthesize ATP. In contrast, lack of Cox3 limits the biosynthesis of COX but does not alter the structure of the enzyme. Consequently, the diminished mitochondrial content of COX and non-functional ATP synthase prevent most mitochondrial ATP production. The biochemical effects caused by the 9205delTA microdeletion displayed a pronounced threshold effect above ∼90% mutation heteroplasmy. We observed a linear relationship between the decrease in subunit Fo-a or Cox3 content and the functional presentation of the defect. Therefore we conclude that the threshold effect originated from a gene–protein level.

The influence of chronic ethanol feeding to rats on liver mitochondrial membrane structure and function

1980 ◽  
Vol 58 (10) ◽  
pp. 1147-1155 ◽  
Author(s):  
E. A. Hosein ◽  
Hung Lee ◽  
Ilan Hofmann
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Rat Liver ◽  
Mitochondrial Membrane ◽  
Membrane Structure ◽  
Membrane Lipids ◽  
Specific Activity ◽  
Structure And Function ◽  
Membrane Structure And Function ◽  
And Function

Arrhenius plots were generated on the activity of rat liver mitochondrial cytochrome c oxidase from Metrecal–sucrose fed controls and Metrecal–alcohol fed experimentals. Chronic alcohol feeding resulted in diminished specific activity of cytochrome c oxidase and abolition of the discontinuity temperature at 17.5 °C found in the controls. Twenty-four hours after alcohol withdrawal, a discontinuity temperature reappeared at 14.4 °C; at 48 h it increased to 22.6 °C and returned to normal (17.4 °C) at 72 h. Such liver mitochondria also showed a decreased capacity to oxidize the acetyl group of acetyl carnitine immediately following prolonged alcohol feeding. When the assay was performed following withdrawal from alcohol 24 h later, oxidation was enhanced and this effect persisted for another 48 h. These latter results revealed a diminished capacity of such mitochondria to oxidize short chain fatty acids during alcohol feeding and the reverse during alcohol withdrawal.These results, complemented by thermographic data obtained through differential scanning calorimetry (DSC) reinforced the view that chronic alcoholic feeding induced adaptive changes in the fluidity of rat liver mitochondrial membrane lipids. Moreover, they demonstrated that in the microenvironment of the membrane-bound enzymes on withdrawal from ethanol, the membrane readapts to the new conditions without alcohol. This involved modulation of membrane structure and function and at the same time demonstrated a role for the membrane in the expression of tolerance and functional dependence on alcohol.

Structure and function of the mitochondrial ubiquinol: cytochrome c reductase and NADH: ubiquinone reductase

1987 ◽  
Vol 15 (1) ◽  
pp. 100-102 ◽  
Author(s):  
HANNS WEISS ◽  
PETRA LINKE ◽  
HORST HAIKER ◽  
KEVIN LEONARD
Keyword(s):  
Cytochrome C ◽  
Structure And Function ◽  
Cytochrome C Reductase ◽  
And Function
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