scholarly journals A new carbon monoxide-induced complex of cytochrome c oxidase

1978 ◽  
Vol 175 (3) ◽  
pp. 1147-1150 ◽  
Author(s):  
P Nicholls
Keyword(s):  
Carbon Monoxide ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Mixed Valence ◽  
Difference Spectrum ◽  
Absorption Bands ◽  
Compound C

Cytochrome c oxidase isolated from ox heart forms a complex in the presence of millimolar concentrations of CO with absorption bands at 606, 565 and 435 nm (difference spectrum), distinct from both ferrocytochrome a and the classical 590nm carbon-monoxyferrocytochrome a3. This species, which closely resembles Compound C, the derivative formed on photolysis and oxygenation of mixed-valence cytochrome a3+a32+CO, may represent a cytochrome a32+CO complex in which the associated (‘invisible’) copper is still oxidized.

scholarly journals Effects of inhibitory ligands on the aerobic carbon monoxide complex of cytochrome c oxidase

1979 ◽  
Vol 183 (3) ◽  
pp. 519-529 ◽  
Author(s):  
P Nicholls
Keyword(s):  
Carbon Monoxide ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Low Temperatures ◽  
Mixed Valence ◽  
Initial Reaction ◽  
Similar Compound ◽  
Compound C ◽  
Alpha Peak ◽  
Oxidative Attack

1. In the presence of both CO and O2, ox heart cytochrome c oxidase forms a 607 nm-peak intermediate distinct from both the cytochrome a2+a3 2+CO and the cytochrome a3+a3 2+CO (‘mixed-valence’) CO complexes. 2. This aerobic CO compound is stable towards ferricyanide addition, but decomposed on treatment with ferric cytochrome a2 ligands such as formate, cyanide and azide. 3. Addition of formate or cyanves rise to a complex with alpha-peak at 598 nm, not identical with any azide complex of the free enzyme, but possibly a cytochrome a3 2+NO complex produced by oxidative attack of partially reduced O2 on the azide. 4. The results support the idea that although the initial reaction of oxygen is with cytochrome a3 2+, the next step is not an oxidation of the ferrous cytochrome a3, but a transfer of O2 to a neighbouring group, such as Cu+, to give Cu2+O2- or similar complexes. 5. The aerobic CO complex is then identified as a3+a3 2+COCu2+O2-; a similar compound (‘Compound C’) is formed by photolysis of a3+a3 2+CO (the ‘mixed-valence’ CO complex) in the presence of oxygen at low temperatures.

scholarly journals S11.25 X-ray structure of carbon monoxide at copper site of the dinuclear site of cytochrome c oxidase

2008 ◽  
Vol 1777 ◽  
pp. S71
Author(s):  
Kazumasa Muramoto ◽  
Naoki Nakagawa ◽  
Maki Taniguchi ◽  
Katsumasa Kanda ◽  
Kyoko Shinzawa-Itoh ◽  
...  
Keyword(s):  
Carbon Monoxide ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
X Ray ◽  
Copper Site

Carbon Monoxide Specifically Inhibits Cytochrome C Oxidase of Human Mitochondrial Respiratory Chain

2003 ◽  
Vol 93 (3) ◽  
pp. 142-146 ◽  
Author(s):  
Jose-Ramon Alonso ◽  
Francesc Cardellach ◽  
Sònia López ◽  
Jordi Casademont ◽  
Òscar Miró
Keyword(s):  
Carbon Monoxide ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Respiratory Chain ◽  
Mitochondrial Respiratory Chain ◽  
Mitochondrial Respiratory

scholarly journals Proton linkage of cytochrome a oxidoreduction in carbon monoxide-treated cytochrome c oxidase

1999 ◽  
Vol 1412 (2) ◽  
pp. 184-189 ◽  
Author(s):  
Michael I Verkhovsky ◽  
Nikolai Belevich ◽  
Joel E Morgan ◽  
Mårten Wikström
Keyword(s):  
Carbon Monoxide ◽  
Cytochrome C ◽  
Cytochrome C Oxidase

Temperature dependence of the reduction potential in CuA in carbon monoxide-inhibited cytochrome c oxidase

Biochemistry ◽  
1986 ◽  
Vol 25 (1) ◽  
pp. 167-171 ◽  
Author(s):  
Hsin Wang ◽  
David F. Blair ◽  
Walther R. Ellis ◽  
Harry B. Gray ◽  
Sunney I. Chan
Keyword(s):  
Carbon Monoxide ◽  
Cytochrome C ◽  
Temperature Dependence ◽  
Cytochrome C Oxidase ◽  
Reduction Potential

scholarly journals Mitochondrial oxygenation of carbon monoxide

1986 ◽  
Vol 239 (1) ◽  
pp. 225-227 ◽  
Author(s):  
L J Young ◽  
W S Caughey
Keyword(s):  
Carbon Monoxide ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
State University ◽  
Co Poisoning ◽  
Colorado State University

A variety of mitochondria have been observed to oxidize 13CO to 13CO2 in the presence of dioxygen, and on the basis of earlier studies [Young & Caughey (1986) Biochemistry 25, 152-161; Young (1981) Ph.D. Dissertation, Colorado State University] this activity is attributed to cytochrome c oxidase. Implications of these findings in respect of some aspects of the pathological biochemistry of CO poisoning are discussed.

scholarly journals Low-temperature kinetics of the reaction of oxygen and solubilized cytochrome oxidase

1978 ◽  
Vol 171 (3) ◽  
pp. 787-798 ◽  
Author(s):  
B Chance ◽  
C Saronio ◽  
J S Leigh ◽  
W J Ingledew ◽  
T E King
Keyword(s):  
Cytochrome Oxidase ◽  
Mixed Valence ◽  
Similar Species ◽  
Absorption Bands ◽  
Compound C ◽  
Valence States ◽  
Membrane Bound ◽  
Peroxy Compounds ◽  
Band Characteristic ◽  
Kinetics Of

The reaction of solubilized cytochrome oxidase in the fully reduced state with O2 at low temperatures reveals components with characteristics similar to those observed with the membrane-bound oxidase, namely compounds A and B, which are proposed to be ‘oxy’ and ‘peroxy’ compounds respectively. Similar species are identified in both solubilized and membrane-bound oxidases; the reaction velocity constant for the reation with O2 and the dissociation constant are decreased 2-3-fold in the solubilied preparation as compared with the membrane-bound species, owing to decreased reactivity towards O2 in the former. The oxidase prepared in the mixed-valence state shows the distinctive absorption band characteristic of compound C, identified in the membrane-bound oxidase. The assignment of the alpha, beta, gamma and near-i.r. absorption bands to possible valence states of these compounds is made.

Sign in / Sign up

Export Citation Format

Share Document