Cytochrome oxidase heme-protein dynamics: a transient Raman study of carbon monoxide photolysis from cytochrome a3

1984 ◽  
Vol 106 (19) ◽  
pp. 5736-5738 ◽  
Author(s):  
E. W. Findsen ◽  
Mark R. Ondrias
Keyword(s):  
Carbon Monoxide ◽  
Cytochrome Oxidase ◽  
Protein Dynamics ◽  
Heme Protein ◽  
Raman Study

Differences between Protein Dynamics of Hemoglobin upon Dissociation of Oxygen and Carbon Monoxide

2012 ◽  
Vol 134 (3) ◽  
pp. 1434-1437 ◽  
Author(s):  
Yuka Murakawa ◽  
Masako Nagai ◽  
Yasuhisa Mizutani
Keyword(s):  
Carbon Monoxide ◽  
Protein Dynamics

Dual pathways of heme protein model compound reactions with carbon monoxide

1976 ◽  
Vol 98 (11) ◽  
pp. 3395-3396 ◽  
Author(s):  
John Cannon ◽  
Jon Geibel ◽  
Martha Whipple ◽  
T. G. Traylor
Keyword(s):  
Carbon Monoxide ◽  
Model Compound ◽  
Heme Protein ◽  
Protein Model

Heme-carbon monoxide religation in photolyzed hemoglobin: a time-resolved Raman study of the iron-carbon monoxide stretching mode

Biochemistry ◽  
1993 ◽  
Vol 32 (5) ◽  
pp. 1318-1323 ◽  
Author(s):  
M. C. Schneebeck ◽  
L. E. Vigil ◽  
J. M. Friedman ◽  
M. D. Chavez ◽  
M. R. Ondrias
Keyword(s):  
Carbon Monoxide ◽  
Time Resolved ◽  
Hemoglobin A ◽  
Raman Study

INHIBITION OF MYOCARDIAL CYTOCHROME OXIDASE FOLLOWING CARBON MONOXIDE EXPOSURE.

2005 ◽  
Vol 33 ◽  
pp. A52
Author(s):  
Kelechi N Iheagwara ◽  
David A Piel ◽  
Richard J Levy ◽  
Clifford S Deutschman ◽  
Stephen R Thom
Keyword(s):  
Carbon Monoxide ◽  
Cytochrome Oxidase

scholarly journals THE EQUILIBRIUM BETWEEN CYTOCHROME OXIDASE AND CARBON MONOXIDE

1957 ◽  
Vol 40 (4) ◽  
pp. 593-608 ◽  
Author(s):  
George Wald ◽  
David W. Allen
Keyword(s):  
Carbon Monoxide ◽  
Cytochrome Oxidase ◽  
Hill Equation ◽  
Bohr Effect ◽  
Degree Of Saturation ◽  
Percentage Saturation ◽  
Equilibrium Function ◽  
Hyperbolic Equilibrium ◽  
High Degree ◽  
The Hill

An evolution argument which attempted to trace the development of hemoglobins from such respiratory pigments as cytochrome oxidase presupposed that the latter possesses, in addition to its high affinity for oxygen, an approximately hyperbolic equilibrium function, and little if any Bohr effect (decline in affinity for oxygen with rise in acidity). Since cytochrome oxidase, unlike hemoglobin, is irreversibly oxidized by oxygen, the present experiments examine its combination with carbon monoxide, with which, like hemoglobin, it yields a true equilibrium. In all known hemoglobins the form of the equilibrium function and the vigor of the Bohr effect are similar with carbon monoxide and with oxygen, so that observations involving the former gas are relevant to the relations of the latter. The equilibrium function of cytochrome oxidase with carbon monoxide—percentage saturation vs. partial pressure of CO—is slightly inflected (in the Hill equation n = 1.26; for a hyperbola, n = 1). No Bohr effect is present in the range of pH 7–8. The pressure of carbon monoxide at which half-saturation occurs (p50) is about 0.17 mm. at 10–13°C. The affinity for carbon monoxide is therefore higher than commonly supposed. These properties are consistent with the evolution argument. They are important also for the physiological functioning of cytochrome oxidase, the nearly hyperbolic equilibrium function facilitating a high degree of saturation, and the lack of Bohr effect making this enzyme impervious to hyperacidity. The slight inflection of the equilibrium function shows that the Fe-porphyrin units of cytochrome oxidase interact to a degree, hence that the enzyme must contain more than one such unit per molecule. It is suggested that in cytochrome oxidase two Fe-porphyrin groups may unite with one oxygen in the manner Fe++-O2-Fe++; and that the evolution of hemoglobins proceeded over a first stage in which the hemes were separated so that each combines with only one molecule of oxygen, so tending to remain reduced; to a further stage in which the separated hemes interact through the protein to facilitate one another in combining with oxygen.

Does carbon monoxide inhibit cytochrome oxidase in vivo?

1997 ◽  
Vol 25 (3) ◽  
pp. 406S-406S
Author(s):  
NATHAN A. DAVIES ◽  
CHRISTOS TRIKKAS ◽  
CHRIS E. COOPER
Keyword(s):  
Carbon Monoxide ◽  
Cytochrome Oxidase

MYOCARDIAL CYTOCHROME OXIDASE INHIBITION FOLLOWING CARBON MONOXIDE EXPOSURE

Shock ◽  
2006 ◽  
Vol 25 (Supplement 1) ◽  
pp. 79
Author(s):  
KN Iheagwara ◽  
SR Thom ◽  
CS Deutschman ◽  
RJ Levy
Keyword(s):  
Carbon Monoxide ◽  
Cytochrome Oxidase ◽  
Oxidase Inhibition
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