The N-benzoyl isocyanide group: A .pi.-acceptor ligand similar to carbon monoxide and a new route to optically active chromium(0) complexes

1979 ◽  
Vol 18 (11) ◽  
pp. 3167-3170 ◽  
Author(s):  
G. Simonneaux ◽  
P. Le Maux ◽  
G. Jaouen ◽  
R. Dabard
Keyword(s):  
Carbon Monoxide ◽  
Optically Active ◽  
Group A

Application of Perfluorooctylbromide Nanoparticles with Ulinastatin for Early Brain Injury Caused by Carbon Monoxide Poisoning

2021 ◽  
Vol 13 (7) ◽  
pp. 1383-1390
Author(s):  
Guangcong Li ◽  
Dan Li
Keyword(s):  
Carbon Monoxide ◽  
Particle Size ◽  
Treatment Group ◽  
Cell Apoptosis ◽  
High Speed ◽  
Carbon Monoxide Poisoning ◽  
Neuronal Cell ◽  
Early Brain Injury ◽  
Group A ◽  
The Brain

ABSTRACTThis study aimed to explore the mechanism of perfluorooctylbromide (PFOB) nanoparticles (NPs) combined with ulinastatin (UTI) on early brain injury (EBI) caused by carbon monoxide poisoning (CMP). Firstly, PFOB NPs were prepared by high-speed dispersion and high-speed homogenization. The physicochemical characteristics of the particle size distribution and Zeta potential distribution of the NPs were analyzed using a laser particle size analyzer. The thermal and photoinduced phase transition characteristics of the NPs were analyzed under heating and laser irradiation conditions. Then, 50 Sprague Dawley (SD) rats were deemed as the research objects to establish the CMP rat models using hyperbaric oxygen chambers. According to different treatment methods, they were rolled into a healthy control group, a carbon monoxide (CO) model group, a PTOB treatment group, an UTI treatment group, and a PTOB + UTI treatment group. The brain tissues of each group of rats were collected 3 days after treatment. The neuronal cell apoptosis, expression of Caspase-3, messenger ribonucleic acid (mRNA) of inflammatory factors interleukin-1β (IL-1β) and tumor necrosis factor-α (TNF-α) in rat brain tissue were detected through immunohistochemical staining, in situ cell apoptosis detection, Reverse transcription-polymerase chain reaction (RT-PCR), and Western blotting, so did the relative expression of target proteins B-cell lymphoma-2 (Bcl-2), Bcl2-Associated X (Bax) and myelin basic protein (MBP). As a result, the average particle size and the average Zeta potential of the prepared PFOB NPs was 103±31 nm and −23 ± 15 mV, respectively. When the PFOB NPs were heated to 80 °C, the particle size increased greatly and cracks appeared. The particle size of PFOB NPs also increased obviously after laser irradiation, and the PFOB inside the particles changed into gas phase. Compared to CO group, expression of Caspase-3, neuronal cell apoptosis rate, mRNA expression of IL-1β and TNF-α, and protein expression of Bax and Bcl-2 in the brain tissue of PTOB group, UTI group, and PFOB + UTI group were notably decreased (P < 0.05), while the MBP protein expression increased considerably (P < 0.05). Changes in PFOB + UTI group were more obvious than those in PTOB group and UTI group, and those indicators weren’t considerably different from the controls. In summary, PFOB NPs were successfully prepared with favorable phase transition characteristics. Moreover, PFOB NPs combined with UTI could reduce the apoptosis of brain neurons after CMP, improve the inflammatory response, and play a protective effect on EBI of CMP.

Palladium-catalyzed alternating copolymerization of carbon monoxide with olefins bearing carbamate and amide functionalities

2001 ◽  
Vol 79 (5-6) ◽  
pp. 587-592 ◽  
Author(s):  
Christophe Moineau ◽  
Giuseppe Mele ◽  
Howard Alper
Keyword(s):  
Carbon Monoxide ◽  
Optically Active ◽  
New Class ◽  
Palladium Catalyzed ◽  
Alternating Copolymerization

The copolymerization of carbon monoxide with different olefins bearing carbamate and amide functionalities was effected using [Pd(CH3CN)4](BF4)2 as the catalyst and (R,R)-Me-DUPHOS (2:1 (v/v) MeNO2–MeOH or CH2Cl2 as the solvent). The products constitute a new class of functionalized copolymers, and were found to be optically active with a mixture of 1,4-ketone and spiroketal repeating units in the backbone. The influence of different parameters on the copolymerization of methyl N-(3-butenyl)carbamate with carbon monoxide was examined.Key words: copolymerization, carbon monoxide, olefins bearing carbamate and amide functionalities.

Copolymerization of 7-Methylenebicyclo[4.1.0]heptane with Carbon Monoxide Initiated by Optically Active Palladium Complexes

2006 ◽  
Vol 89 (8) ◽  
pp. 1574-1588 ◽  
Author(s):  
Daisuke Takeuchi ◽  
Ayami Yasuda ◽  
Takeshi Okada ◽  
Junpei Kuwabara ◽  
Kohtaro Osakada ◽  
...  
Keyword(s):  
Carbon Monoxide ◽  
Palladium Complexes ◽  
Optically Active

Haem a compounds as models for cytochromes of group a - I. Absorption spectra of haem a compounds with proteins and other nitrogenous ligands

1962 ◽  
Vol 155 (960) ◽  
pp. 339-355 ◽  
Keyword(s):  
Carbon Monoxide ◽  
Molecular Oxygen ◽  
Absorption Spectra ◽  
Bovine Serum ◽  
Soret Band ◽  
Horse Radish Peroxidase ◽  
Serum Albumins ◽  
Group A

Absorption spectra of ferrous and ferric haem a and haem a compounds with nitrogenous ligands (pyridine, 4-methylimidazole, cyanide, human and bovine serum albumins, human apohaemoglobin, horse apomyoglobin and horse-radish apoperoxidase) as well as their carbon monoxide compounds are described. The absorption spectra of the haemoproteins provide a good model for bacterial cytochrome a 1 , but not for cytochrome a and especially not for cytochrome a 3 . Both cytochromes a and a 3 differ from the model haemoproteins in the position of the α -band of the ferrous compound. Cytochrome a 3 differs from them, moreover, in that carbon monoxide shifts its α -band towards the blue, not towards the red, and in its much higher ratio of extinction of the Soret band to that of the α -band. The type of linkage of a protein to haematin a appeared to differ in several instances from the type of linkage of the same protein to protohaematin. The characteristic spectroscopic differences between haemoglobin, haemalbumin and haemochromes, or between human and bovine haemalbumin, found in the protohaem series, are absent in the haem a series. We have found no evidence for a reversible combination of haem a -globin with molecular oxygen; nor had the compound of haem a with the apoenzyme of horse-radish peroxidase strong peroxidative activity.

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