scholarly journals Iso-cytochrome c species from baker's yeast. Analysis of their circular-dichroism spectra

1976 ◽  
Vol 157 (3) ◽  
pp. 773-775 ◽  
Author(s):  
Y Looze ◽  
E Polastro ◽  
C Gielens ◽  
J Léonis
Keyword(s):  
Circular Dichroism ◽  
Cytochrome C ◽  
Visible Region ◽  
Helical Structure ◽  
Baker’S Yeast ◽  
Baker's Yeast ◽  
Circular Dichroism Spectra ◽  
Horse Heart Cytochrome ◽  
Horse Heart Cytochrome C ◽  
Circular Dichroïsm

The circular-dichroism spectra of baker's-yeast iso-1- (methylated and unmethylated forms) and iso-2-cytochrome c species were examined between 200 and 600nm. In the visible region the yeast haemoproteins have characteristics nearly indistinguishable from those of horse heart cytochrome c. From the spectra in the u.v. region the latter appears, however, to be more helical. It is proposed that the likely element of non-helical structure in iso-1-cytochrome c is residues 62-70.

Influence of glycerol on the structure and redox properties of horse heart cytochrome c. A circular dichroism and electrochemical study

1996 ◽  
Vol 15 (7) ◽  
pp. 599-606 ◽  
Author(s):  
Giampiero De Sanctis ◽  
Alessandra Maranesi ◽  
Tommaso Ferri ◽  
Alessandro Poscia ◽  
Franca Ascoli ◽  
...  
Keyword(s):  
Circular Dichroism ◽  
Cytochrome C ◽  
Redox Properties ◽  
Electrochemical Study ◽  
Horse Heart Cytochrome ◽  
Horse Heart Cytochrome C ◽  
Circular Dichroïsm

Circular dichroism spectra of amino acid complexes. II. Chelated amino acid complexes with the CoN5O chromophore

1970 ◽  
Vol 23 (9) ◽  
pp. 1735 ◽  
Author(s):  
CJ Hawkins ◽  
PJ Lawson
Keyword(s):  
Amino Acids ◽  
Circular Dichroism ◽  
Amino Acid ◽  
Visible Region ◽  
Optically Active ◽  
Circular Dichroism Spectra ◽  
Amino Acid Complexes ◽  
Similar Series ◽  
Cotton Effects ◽  
Circular Dichroïsm

The circular dichroism spectra of a series of optically active (α-aminocarboxylato)tetraamminecobalt(111) complexes have been measured in aqueous solution, and in the presence of salts of polarizable anions. The observed spectra in the visible region have been analysed to determine the signs of the Cotton effects of the three components of the 1A1g ↔ 1T1g cobalt(111) transition. For L-amino acids, the transition with A2g(D4h) parentage is negative, and the two transitions with Eg(D4h) parentage have opposite signs. Published circular dichroism spectra of complexes of the type [Co(en)2(L-am)]2+ were similarly interpreted in terms of a perturbed tetragonal chromophore, and it was shown that the vicinal effect of the L-amino acids imposed the same signs onto the component transitions as for the tetraammines and for a similar series of pentaamminecobalt(111) complexes.

scholarly journals Magnetization curves of haemoproteins measured by low-temperature magnetic-circular-dichroism spectroscopy

1980 ◽  
Vol 191 (2) ◽  
pp. 411-420 ◽  
Author(s):  
A J Thomson ◽  
M K Johnson
Keyword(s):  
Circular Dichroism ◽  
Cytochrome C ◽  
High Spin ◽  
Ground State ◽  
Magnetic Circular Dichroism ◽  
Striking Difference ◽  
Zero Field ◽  
Magnetization Curves ◽  
Horse Heart Cytochrome ◽  
Circular Dichroïsm

The magnetic-circular-dichroism (m.c.d.) spectra of methymyoglobin cyanide and oxidized horse heart cytochrome c were measured in the region of the Soret band over a range of temperatures from 1.5 to 50 K and in fields from 0 to 5T. A similar study has been made with reduced bovine heart cytochrome c oxidase, which contains one high-spin ferrous haem, namely a3. M.c.d. magnetization curves characteristic of an isolated Kramer's ground state with spin S = 1/2. These curves contrast with the magnetization curve of the high-spin ferrous haem with spin S = 2. The electronic ground state of the latter compound contains zero-field components that are thermally accessible over the temperature range of the experiment. Hence the magnetization curves are a complex nested set. The magnetization curves of the S = 1/2 proteins were analysed and it is shown that it is possible to make estimates of the ground-state g-factors even in the presence of rhombic anisotropy, provided that some knowledge of the polarizations of the electronic transitions is available. The striking difference between the m.c.d. magnetization curves of a simple S = 1/2 paramagnet and magnetically complex ground state should prove extremely useful when m.c.d. spectroscopy is sued to probe the magentic properties of metal centres in proteins, and should have wide application beyond the field of haemoproteins.

Circular dichroism spectra of cytochrome c oxidase

Metallomics ◽  
2011 ◽  
Vol 3 (4) ◽  
pp. 417 ◽  
Author(s):  
Artem V. Dyuba ◽  
Alexander M. Arutyunyan ◽  
Tatiana V. Vygodina ◽  
Natalia V. Azarkina ◽  
Anastasia V. Kalinovich ◽  
...  
Keyword(s):  
Circular Dichroism ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Circular Dichroism Spectra ◽  
Circular Dichroïsm
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