Energy Medicine
Len Wisneski in The Scientific Basis of Integrative Health, 2017
The biophysical process of laser absorption into cells of the soft or hard tissue is identical, except that with a suitable selection of wavelength and pulse energies, virtually all laser energy can be converted into bioelectronic and biochemical energy, thus avoiding thermal tissue damage. This photonic to electronic conversion occurs in the mitochondria of cells via the enzyme, cytochrome c oxidase, which is one of the main intracellular chromophores (Karu, 1999; Karu and Afanas 1995). Cytochrome c oxidase is a large mitochondrial membrane protein of considerable complexity that catalyzes the final step in the mitochondrial respiratory chain (i.e., in the transfer of electrons to molecular oxygen causing its chemical reduction into water) (Karu, 2007) (Figure 10.6).
Structural Studies of Copper Proteins Using X-Ray Absorption Spectroscopy
René Lontie in Copper Proteins and Copper Enzymes, 1984
Cytochrome c oxidase50 is the membrane-bound enzyme involved in the terminal step of mitochondrial respiration. The enzyme plays an extremely important role in electron transport (catalysing the reduction of dioxygen to water) and in bioenergetics (as a proton pump). It is a relatively large enzyme (Mr approximately 150,000) containing two heme irons and two copper ions. The two iron sites are denoted as cytochrome a and cytochrome a3, and the copper sites denoted as CuA and CuB. CuB and the heme iron of cytochrome a3, which are both EPR silent, are believed to be antiferromagnetically coupled. X-ray absorption studies19,51–55 have been reported on both copper and iron, but only the copper work will be reviewed here.
The minerals
Geoffrey P. Webb in Nutrition, 2019
There are a number of important copper-containing proteins in the body and these include: Some types of superoxide dismutase which is involved in free radical disposal (see Chapter 13). Enzymes involved in the synthesis of the catecholamine group of nerve transmitters from tyrosine (e.g. adrenalin, noradrenalin and dopamine). Enzymes involved in the synthesis of the pigment melanin responsible for, amongst other things, skin pigmentation. Cytochrome c oxidase involved in the electron transfer system in mitochondria. Ceruloplasmin which is involved in the transport and oxidation of iron that is necessary for haemoglobin synthesis.
Really does temperature reduction and norepinephrine have similar effects on the energy metabolism in rat brown adipose tissue?
Published in Archives of Physiology and Biochemistry, 2018
B. Sopeña, Z. López-Ibarra, A. J. López-Farré, N. de las Heras, S. Ballesteros, A. González-Cantalapiedra, V. Lahera, J. J. Zamorano-León
The presence of norepinephrine during temperature reduction in BAT maintained UCP-1 up-expression and mitochondrial F1 ATP synthase α-chain down-expression observed by reducing temperature alone. In addition, the presence of norepinephrine during exposition of BAT to reducing temperature also diminished the protein expression level of cytochrome c oxidase with respect to 37 °C-incubated BAT. Under normal physiological conditions, cytochrome c oxidase acts as rate-limiting step of respiratory chain. In this regard, Kadenbach's hypothesis states that the regulation of the membrane potential and ROS formation in mitochondria are determined by the ATP-induced allosteric inhibition of cytochrome c oxidase and represents a mechanism for respiratory control (Kadenbach et al.2009). Under maximal stress conditions, as it may occur in BAT by the presence of norepinephrine during temperature reduction, cytochrome c oxidase losses its allosteric inhibition by ATP and cytochrome c oxidase activity remained increased. In addition, under these conditions the mitochondrial membrane potential was also increased favouring mitochondrial ROS formation (Vogt et al.2016). Therefore, in BAT exposed to temperature reduction, the down expression of cytochrome c oxidase by norepinephrine may act as protective mechanism to reduce mitochondrial ROS generation through the mitochondrial respiratory chain. In this regard, activated thermogenesis in BAT was demonstrated to increase mitochondrial ROS production levels (Chouchani et al.2016).
Cytochrome c injection induced embryo loss
Published in Drug and Chemical Toxicology, 2021
Tonghui Xu, Qiuhong Yang, Banqin Wang, Wenfu Wang, Jingxin Li, Yuyan Ma, Xiaolin Gao
Cytochrome c plays an important role in electron transfer between cytochrome c oxidase and reductase (Margalit and Schejter 1973). Normally, cytochrome c resides between the inner and outer mitochondrial membrane. At present, cytochrome c has been used as first-aid in the clinic for organs which are lacking oxygen. However, intriguingly based on more recent evidence, injection of cytochrome C has been shown to result in selective suicide of dendritic cells (DCs) (Lin et al.2008) and failure of self-tolerance (Qiu et al.2009). It is widely believed that decidual antigen-presenting cells (APCs), especially DCs, are critical for fetomaternal tolerance (Blois et al.2004, Blois et al.2007). In vivo DCs depletion affects implantation and early placental development in mice (Krey et al.2008). Cross talk between DCs and natural killer cells at the feto-maternal interface is also believed to be pivotal for pregnancy (Laskarin et al.2007). As a failure of self-tolerance result, recurrent spontaneous abortion (RSA) occurs in pregnant women. This type of abortion has been related to a shift in the T helper 2 (Th2) cell response of normal pregnancy to a Th1 response, where cytokines such as interferon-γ (INF-γ) and tumor necrosis factor-α (TNF‐α) can destroy trophoblasts (Raghupathy 1997). Therefore, we hypothesized that transient ablation of decidual DCs by cytochrome c injection may result in failed fetomaternal tolerance induction and Th1/Th2 imbalances, triggering embryo loss and abortion.
Can isosorbide dinitrate oral spray serve as an immediate bridging therapy for a mass cyanide poisoning?
Published in Clinical Toxicology, 2021
Ophir Lavon, Gary A. Rockwood, Arik Eisenkraft
The potential mechanism of antidotal action of ISDN is not totally clear. It is evident that ISDN is not a methemoglobin former; its administration does not result in any significant rise in methemoglobin levels, either in swine, rabbits or humans [2,6–8,14]. ISDN in the body is rapidly reduced to nitric oxide (NO) through a NO synthase-independent pathway [15]. It was previously shown that NO carries antidotal properties against cyanide, specifically in the mitochondrial electron transport chain. NO competes with cyanide for binding to cytochrome C oxidase [15,16]. Both direct or non-direct (through sodium nitrite) NO administration mitigated the inhibition of cytochrome C oxidase by cyanide [16–18]. In addition, NO is neuroprotective mainly by reducing hyperactivity of NMDA receptors in the brain [7,19–21]. This may prevent or counteract the effects of cyanide on the central nervous system, clinically expressed as coma, seizures and respiratory depression.
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