ChemInform Abstract: THE CHEMISTRY OF PYRROLIC COMPOUNDS. PART 56. PORPHYRINS AND RELATED MACROCYCLES. PART 24. ISOLATION, CRYSTALLIZATION, AND SYNTHESIS OF THE DIMETHYL ESTER OF PORPHYRIN A, THE IRON-FREE PROSTHETIC GROUP OF CYTOCHROME C OXIDASE

1985 ◽  
Vol 16 (17) ◽  
Author(s):  
A. R. BATTERSBY ◽  
E. MCDONALD ◽  
M. THOMPSON ◽  
I. A. CHAUDHRY ◽  
P. S. CLEZY ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Dimethyl Ester ◽  
Prosthetic Group

Isolation, crystallisation, and synthesis of the dimethyl ester of porphyrin a, the iron-free prosthetic group of cytochrome c oxidase

1985 ◽  
pp. 135 ◽  
Author(s):  
Alan R. Battersby ◽  
Edward McDonald ◽  
Mervyn Thompson ◽  
Irshad A. Chaudhry ◽  
Peter S. Clezy ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Dimethyl Ester ◽  
Prosthetic Group

Cytochrome C oxidase: isolation, crystallisation, and synthesis of porphyrin a dimethyl ester

1977 ◽  
pp. 278 ◽  
Author(s):  
Mervyn Thompson ◽  
Jack Barrett ◽  
Edward McDonald ◽  
Alan R. Battersby ◽  
Christopher J. R. Fookes ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Dimethyl Ester

scholarly journals Heme-a, the heme prosthetic group of cytochrome c oxidase, is increased in Alzheimer's disease

2009 ◽  
Vol 461 (3) ◽  
pp. 302-305 ◽  
Author(s):  
Barney E. Dwyer ◽  
Meghan L. Stone ◽  
Nadia Gorman ◽  
Peter R. Sinclair ◽  
George Perry ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Prosthetic Group ◽  
Heme Prosthetic Group

Cytochrome c and cytochrome c oxidase interactions: the effects of ionic strength and hydrostatic pressure studied with site-specific modifications of cytochrome c

1992 ◽  
Vol 70 (7) ◽  
pp. 539-547 ◽  
Author(s):  
Jack A. Kornblatt ◽  
Janice Theodorakis ◽  
Gaston Hui Bon Hoa ◽  
Emmanuel Margoliash
Keyword(s):  
Hydrostatic Pressure ◽  
Cytochrome C ◽  
Cytochrome Oxidase ◽  
Cytochrome C Oxidase ◽  
Front Surface ◽  
Prosthetic Group ◽  
Binding Interaction ◽  
Cytochromes C ◽  
Heme Prosthetic Group ◽  
Full Charge

Seven cytochromes c, in which individual lysines have been modified to the propylthiobimane derivatives, have been prepared. These derivatives were also converted to the porphyrin cytochromes c by treatment with HF. The properties of both types of modified proteins were studied in their reactions with cytochrome c oxidase. The results show that lysines 25, 27, 60, 72, and 87 do not contribute a full charge to the binding interaction with the oxidase. These five residues, with the exception of the lysine-60 derivative, are on the front surface of the protein and contain the solvent-accessible edge of the heme prosthetic group. By contrast, lysines 8 and 13 at the top of the front surface do contribute a full charge to the binding interaction with the oxidase. The removal of the positive charge on any one lysine weakens the binding to cytochrome c oxidase by at least 1 kcal (1 cal = 4.1868 J). The presence of bimane at lysines 13 and 87 clearly forces the separation of the cytochrome c and oxidase, but this does not occur with the other complexes. The bimane-modified lysine-13 protein, and to a lesser extent that modified at lysine 8, show the interesting effect of enhanced complex formation with cytochrome c oxidase when subjected to pressure, possibly because of entrapment of water at the newly created interface of the complex. Our observations indicate that the two proteins of the cytochrome c – cytochrome oxidase complex have preferred, but not obligatory, spatial orientations and that interaction occurs without either protein losing significant portions of its hydration shell.Key words: cytochrome oxidase, cytochrome c, binding, hydrostatic pressure.

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