A new route to carbon monoxide adducts of heme proteins

2008 ◽  
Vol 12 (10) ◽  
pp. 1096-1099 ◽  
Author(s):  
Sergei V. Makarov ◽  
Denis S. Salnikov ◽  
Anna S. Pogorelova ◽  
Zoltan Kis ◽  
Radu Silaghi-Dumitrescu
Keyword(s):  
Carbon Monoxide ◽  
Cytochrome C ◽  
Heme Proteins ◽  
Single Step ◽  
Anaerobic Conditions ◽  
Large Excess ◽  
Thiourea Dioxide ◽  
Hydrolysis Of ◽  
Protein Moiety ◽  
Co Gas

Sulfoxylate SO 2 H −( SO 22−), a strong reducing agent readily produced by hydrolysis of thiourea dioxide, reacts with ferric myoglobin ( Mb ) to reversibly produce Fe (II)- Mb , starting from either aerobic or anaerobic conditions. Exposure of Fe (II)- Mb to excess sulfoxylate further produces Fe (II)- CO - Mb . Fe (II)- Mb can be regenerated by reoxidation with ferricyanide at this stage; hemin, rubredoxin and cytochrome c show a similar reactivity towards sulfoxylate. The source of CO is not the protein moiety, nor is it the heme or the thiourea dioxide – but rather CO 2, via its reaction with sulfoxylate when the latter is used in large excess. These findings provide a convenient single-step route to carbon monoxide heme adducts, without the need to manipulate toxic CO gas.

CO Surrogates: A Green Alternative in Palladium-Catalyzed CO Gas Free Carbonylation Reactions

2020 ◽  
Vol 24 (22) ◽  
pp. 2588-2600
Author(s):  
Mayur V. Khedkar ◽  
Shoeb R. Khan ◽  
Trimurti L. Lambat ◽  
Ratiram G. Chaudhary ◽  
Ahmed A. Abdala
Keyword(s):  
Carbon Monoxide ◽  
Fine Chemicals ◽  
Large Excess ◽  
Specific Reaction ◽  
Recent Developments ◽  
Palladium Catalyzed ◽  
Direct Use ◽  
Substantial Interest ◽  
Co Gas

Carbonylation reactions with carbon monoxide (CO) provide efficient and attractive routes for the synthesis of bulk and fine chemicals. However, the practice of using a large excess of an inflammable, lethal and greenhouse CO gas is always a concern in this chemistry. The development of CO surrogates has gained substantial interest and become a green alternative to gaseous CO. Many of the recent studies have focused on the development of other benign and safe reagents to work as a CO source in carbonylation reactions, and the assortment of feasible CO surrogates for specific reaction can be accomplished by the literature data. This review describes the recent developments in palladium-catalyzed carbonyl insertions without the direct use of gaseous CO.

Photoactive conjugated polymer/graphdiyne nanocatalyst for CO2 reduce into CO in living cells for hypoxia tumor treatment

2021 ◽  
Author(s):  
Endong Zhang ◽  
Zicheng Zuo ◽  
Wen Yu ◽  
Hao Zhao ◽  
Shengpeng Xia ◽  
...  
Keyword(s):  
Carbon Monoxide ◽  
Photodynamic Therapy ◽  
Tumor Microenvironment ◽  
Conjugated Polymer ◽  
Tumor Therapy ◽  
Living Cells ◽  
Tumor Treatment ◽  
Treatment Efficiency ◽  
Therapy Strategy ◽  
Co Gas

Carbon monoxide (CO) gas therapy has grown to be an emerging tumor therapy strategy to avoid low treatment efficiency of photodynamic therapy (PDT) caused by the hypoxia tumor microenvironment. However,...

scholarly journals Adapting decarbonylation chemistry for the development of prodrugs capable of in-vivo delivery of carbon monoxide utilizing sweeteners as carrier molecules

2021 ◽  
Author(s):  
Ladie Kimberly De La Cruz ◽  
Xiaoxiao Yang ◽  
Anna Menshikh ◽  
Maya Brewer ◽  
Wen Lu ◽  
...  
Keyword(s):  
Carbon Monoxide ◽  
Animal Models ◽  
Therapeutic Agent ◽  
Organ Injury ◽  
Signaling Molecule ◽  
In Vivo Delivery ◽  
Co Gas

Carbon monoxide as an endogenous signaling molecule exhibits pharmacological efficacy in various animal models of organ injury. To address the difficulty in using CO gas as a therapeutic agent for...

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

Rh(I)-Catalyzed CO Gas-Free Carbonylative Cyclization of Organic Halides with Tethered Nucleophiles Using Aldehydes as a Substitute for Carbon Monoxide.

ChemInform ◽  
2007 ◽  
Vol 38 (18) ◽  
Author(s):  
Tsumoru Morimoto ◽  
Masahiko Fujioka ◽  
Koji Fuji ◽  
Ken Tsutsumi ◽  
Kiyomi Kakiuchi
Keyword(s):  
Carbon Monoxide ◽  
Organic Halides ◽  
Co Gas

Reductive Activation of Carbon Tetrachloride by Human Haemoglobin

1993 ◽  
Vol 21 (1) ◽  
pp. 57-64
Author(s):  
Roberta Ferrara ◽  
Michela Rezzadore ◽  
Stefano Cazzaro ◽  
Roberto Tolando ◽  
Maurizio Manno
Keyword(s):  
Carbon Monoxide ◽  
Carbon Tetrachloride ◽  
Anaerobic Incubation ◽  
Reductive Activation ◽  
Anaerobic Conditions ◽  
Prosthetic Group ◽  
Experimental Conditions ◽  
Human Haemoglobin ◽  
Reductive Metabolism

The reductive metabolism of carbon tetrachloride (CC14) by human haemoglobin (Hb) was observed in vitro by absolute absorption spectra recorded under anaerobic conditions. The following results were obtained: 1) a decrease of the 430nm peak typical of free reduced Hb (Hb2+); 2) the formation of a shoulder of absorbance, attributable to the production of a complex between Hb2+ and a metabolite of CC14 carbon monoxide (Hb-CO); and 3) the oxidation of some Hb2+ to methaemoglobin (Hb3+). The concentration of these three forms — Hb2+, Hb-CO and Hb3+ — during anaerobic incubation of Hb with CC14 was calculated algebraically from the absolute spectra. CO production was then calculated from the concentration of Hb-CO, using a suitable calibration curve. Interestingly, under identical experimental conditions, a substrate-dependent loss of Hb-derived haem, but not of Hb itself nor of haem-derived porphyrin fluorescence, was measured. Preliminary HPLC studies to clarify the discrepancy and, in particular, the role and fate of the haem group, showed two substrate-dependent modified haem products. The results indicate that human Hb is able to catalyse the reductive activation of CCl4, and suggest that, during the process, its prosthetic group haem may be modified by CC14 metabolites to products which maintain a tetrapyrrolic structure but are unable to react with pyridine.

scholarly journals Carbon Monoxide Inhibits Tenascin-C Mediated Inflammation via IL-10 Expression in a Septic Mouse Model

2015 ◽  
Vol 2015 ◽  
pp. 1-14 ◽  
Author(s):  
Md. Jamal Uddin ◽  
Chun-shi Li ◽  
Yeonsoo Joe ◽  
Yingqing Chen ◽  
Qinggao Zhang ◽  
...  
Keyword(s):  
Carbon Monoxide ◽  
Proinflammatory Cytokines ◽  
Tissue Injury ◽  
Inflammatory Diseases ◽  
Septic Mouse ◽  
Induced Expression ◽  
Tenascin C ◽  
Co Gas

Tenascin-C (TN-C), an extracellular matrix (ECM) glycoprotein, is specifically induced upon tissue injury and infection and during septic conditions. Carbon monoxide (CO) gas is known to exert various anti-inflammatory effects in various inflammatory diseases. However, the mechanisms underlying the effect of CO on TN-C-mediated inflammation are unknown. In the present study, we found that treatment with LPS significantly enhanced TN-C expression in macrophages. CO gas, or treatment with the CO-donor compound, CORM-2, dramatically reduced LPS-induced expression of TN-C and proinflammatory cytokines while significantly increased the expression of IL-10. Treatment with TN-C siRNA significantly suppressed the effects of LPS on proinflammatory cytokines production. TN-C siRNA did not affect the CORM-2-dependent increase of IL-10 expression. In cells transfected with IL-10 siRNA, CORM-2 had no effect on the LPS-induced expression of TN-C and its downstream cytokines. These data suggest that IL-10 mediates the inhibitory effect of CO on TN-C and the downstream production of proinflammatory cytokines. Additionally, administration of CORM-2 dramatically reduced LPS-induced TN-C and proinflammatory cytokines production while expression of IL-10 was significantly increased. In conclusion, CO regulated IL-10 expression and thus inhibited TN-C-mediated inflammationin vitroandin vivo.

Heme Proteins, Cytochrome c Oxidase

2013 ◽  
pp. 939-944
Author(s):  
Oliver-M. H. Richter ◽  
Bernd Ludwig
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Heme Proteins
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