The axial ligands of heme in cytochromes: a near-infrared magnetic circular dichroism study of yeast cytochromes c, c1, and b and spinach cytochrome f

Biochemistry ◽  
1989 ◽  
Vol 28 (20) ◽  
pp. 8033-8039 ◽  
Author(s):  
David Simpkin ◽  
Graham Palmer ◽  
F. J. Devlin ◽  
M. C. McKenna ◽  
G. M. Jensen ◽  
...  
1981 ◽  
Vol 670 (3) ◽  
pp. 341-354 ◽  
Author(s):  
Toru Shimizu ◽  
Tetsutaro Iizuka ◽  
Hideo Shimada ◽  
Yuzuru Ishimura ◽  
Tsunenori Nozawa ◽  
...  

1982 ◽  
Vol 207 (1) ◽  
pp. 167-170 ◽  
Author(s):  
A J Thomson ◽  
D G Englinton ◽  
B C Hill ◽  
C Greenwood

The magnetic-circular-dichroism (m.c.d.) spectra of oxidized ‘resting’ bovine cytochrome c oxidase and the cyanide-inhibited form are reported at 5.15 T and at 4.2 K along with m.c.d. magnetization curves plotted at selected wavelengths. In both spectra there are features at 790nm and 1564nm due to Cua and haem a respectively, the e.p.r.-detectable components of the enzyme. There is a new peak at 1946nm only in the spectrum of the cyanide-inhibited enzyme. Arguments are advanced that assign this to low-spin ferric haem a3 bridged to Cua3, thereby forming a ferromagnetically coupled pair of metal ions.


1982 ◽  
Vol 55 (10) ◽  
pp. 3059-3063 ◽  
Author(s):  
Takao Yamamoto ◽  
Tsunenori Nozawa ◽  
Nagao Kobayashi ◽  
Masahiro Hatano

Biochemistry ◽  
1977 ◽  
Vol 16 (8) ◽  
pp. 1725-1729 ◽  
Author(s):  
J. Rawlings ◽  
P. J. Stephens ◽  
L. A. Nafie ◽  
M. D. Kamen

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