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.

Abstract 324: An Engineered Protein as an Antidote for Carbon Monoxide Poisoning That Can Reverse Cardiovascular Collapse Through Scavenging of Carbon Monoxide and Rescue of Mitochondrial Respiration

Circulation ◽  
2018 ◽  
Vol 138 (Suppl_2) ◽  
Author(s):  
Jason J Rose ◽  
Qinzi Xu ◽  
Kaitlin A Bocian ◽  
Timothy N Bachman ◽  
Jian Hu ◽  
...  
Keyword(s):  
Carbon Monoxide ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Carbon Monoxide Poisoning ◽  
T Test ◽  
Activity Level ◽  
Tissue Respiration ◽  
Cardiovascular Collapse ◽  
Co Poisoning ◽  
Cardiovascular Dysfunction

Background: Carbon monoxide (CO) is the most common human poisoning. There is no antidote. One-third of hospitalized patients will have cardiac dysfunction and increased mortality. Little is known about the nature of cardiovascular dysfunction during acute CO poisoning. CO toxicity results from: (1) global hypoxia and decreased oxygen delivery through CO binding to hemoglobin, (2) inhibition of oxidative phosphorylation from CO binding to cytochrome c oxidase, and (3) ensuing superoxide injury. We have developed a recombinant neuroglobin molecule (rNgb) with a high affinity for CO, that can chelate CO from intrinsic heme proteins. Hypothesis: The addition of rNgb will scavenge CO from hemoglobin and cytochrome c oxidase, reversing CO-induced cardiovascular dysfunction. Methods: We inserted micromanometer-tip catheters into the left ventricle of ventilated, severely CO poisoned mice to study the mechanisms of CO-induced cardiovascular collapse. In a similar model, we measured blood pressure and heart rate of severely CO poisoned, ventilated mice through a carotid arterial catheter and treated with phosphate buffered saline (PBS) or rNgb. Hearts were isolated from these mice and we measured tissue respiration using a Clark-type oxygen electrode. We compared the respiration rates of these animals and compared with non-poisoned, sedated control mice. We also compared the enzymatic activity of electron transport chain complexes. Results and Conclusions: When compared to control mice (exposed to 21% oxygen/no CO), CO poisoned mice develop a decreased contractility index (-32.3% baseline vs. -10.8% in control, t-test, p=0.002), hypotension and death, indicating primary cardiac toxicity. CO-poisoned mice treated with PBS had heart tissue respiration that was 62.3% (+/- 7.5%) of sedated control mice (t-test, P=0.015). Treatment of mice with rNgb restored tissue respiration (P=0.037 versus PBS treated mice) similar to control values. CO poisoning reduced the activity level of complex IV in PBS treated mice (P=0.011), but levels were similar to control in rNgb treated mice. These molecular changes were associated with reversal of cardiovascular collapse in rNgb treated mice versus PBS, demonstrating the potential of rNgb as a CO poisoning antidote.

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

Oxygenation of carbon monoxide by bovine heart cytochrome c oxidase

Biochemistry ◽  
1986 ◽  
Vol 25 (1) ◽  
pp. 152-161 ◽  
Author(s):  
Lawrence J. Young ◽  
Winslow S. Caughey
Keyword(s):  
Carbon Monoxide ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Bovine Heart

Lymphocyte cytochrome c oxidase, cyclic GMP and cholinergic muscarinic receptors as peripheral indicators of carbon monoxide neurotoxicity after acute and repeated exposure in the rat

Life Sciences ◽  
2006 ◽  
Vol 78 (17) ◽  
pp. 1915-1924 ◽  
Author(s):  
Anna F. Castoldi ◽  
Teresa Coccini ◽  
Giovanna Randine ◽  
Mariluz Hernández-Viadel ◽  
Vicente Felipo ◽  
...  
Keyword(s):  
Carbon Monoxide ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Muscarinic Receptors ◽  
Cyclic Gmp ◽  
Repeated Exposure
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