Sentences with phrase «c oxidase»

The heart of the innovation, as I understand it, lies in the choice of a particular and small region of DNA shared by many animals; to say it in technical terms: it's «a 648 base - pair region in the mitochondrial cytochrome c oxidase 1 gene («CO1»).»

This toxin stops the cell respiration as a non-competitive inhibitor for an enzyme in the mitochondria that is referred to as cytochrome c oxidase, causing asphyxiation in the cells.

In your mitochondria, there's also a specific molecule called cytochrome c oxidase, which is involved in the energy production within the mitochondria.

It helps to stimulate cytochrome c oxidase enzyme and increase ATP (adenosine triphosphate) in your tissue, which is your primary source of high energy production.

It is a cofactor in several oxidative enzymes vital to the function of hematopoietic, vascular and skeletal tissues, as well as the structure and function of the nervous system, including superoxide dismutase (oxygen radical scavenger), cytochrome - c oxidase (mitochondrial respiration), lysyl oxidase (collagen and elastin synthesis) and ceruloplasmin ferroxidase / haephestin (iron metabolism).

The important thing to understand is that LLLT works by activating a very important enzyme known as «cytochrome c oxidase»... which plays a crucial role in healthy metabolism and energy production.

Light therapy (how we use it) helps activate an important metabolic enzyme called cytochrome c oxidase, which is essential for healthy cellular energy production, and relaxation.

Red to infra - red light has been shown to effectively activate an important metabolic enzyme known as cytochrome c oxidase.

It's a function of the protein in the intermitochondrial membrane called uh — Cytochrome C Oxidase which I think most people know.

And Cytochrome C Oxidase is a heme protein just like hemoglobin in our skin.

Hybrid broadband NIRS / Diffuse correlation spectroscopy system for simultaneous monitoring of cerebral perfusion and cytochrome c oxidase

DNA barcoding aims to provide an efficient method for species - level identifications using an array of species specific molecular tags derived from the 5 ′ region of the mitochondrial cytochrome c oxidase I (COI) gene.

Molecular evolution of the cytochrome c oxidase subunit 5A gene in primates.

This protein is one of the nuclear - coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.

Cytochrome c oxidase is part of Complex IV.

A famous example from the superfamily is cytochrome c oxidase, the last enzyme in the respiratory electron transport chain located in the mitochondrial membrane (see graph).

Knockdown of human COX17 affects assembly and supramolecular organization of cytochrome c oxidase.

Chronic treatment with azide in situ leads to an irreversible loss of cytochrome c oxidase activity via holoenzyme dissociation.

They can not replace damaged mitochoondrial proteins, but for the most part, they are pretty resistant to oxidative damage (particularly cytochrome c oxidase which is very oxidative damage resistant, much more so than is DNA).

Adaptive evolution of cytochrome c oxidase: infrastructure for a carnivorous plant radiation Jobson, R. W., R. Nielsen, L. Laakkonen, M. Wikström et al. 2004.

Adaptive evolution of cytochrome c oxidase: infrastructure for a carnivorous plant radiation.

Among the other genes she says play a role in thoroughbred performance are peroxisome proliferator - activated receptor - γ coactivator - 1 alpha (PGC - 1α), which is involved in skeletal muscle adaptation to exercise; pyruvate dehydrogenase kinase, isozyme 4 (PDK4), involved in glucose regulation, expression of which increased almost fourfold after sprints; and cytochrome c oxidase subunit 4 isoform 2 (COX 4I2), involved in respiration.

However, the E. coli bacteria has two types of oxidase: bo - type cytochrome oxidase (analogue of «human» cytochrome - c oxidase) and completely different bd - type cytochromes.

Each cell in our body «breathes» due to the work of only the cytochrome - c oxidase, others we have not.

Not exact matches

For example, Bsl1 itself was highly increased in bsl1 - 1 mutants (corrected P = 0.003), as was a gene encoding a BR C - 6 oxidase orthologous to brassinosteroid deficient1 (brd1) from maize (Makarevitch et al., 2012) and rice (Hong et al., 2002)(SvBrd1; Sevir.9 G171700).

(2012) Brd1 gene in maize encodes a brassinosteroid C - 6 oxidase.

Our inability to synthesize vitamin C is the result of a mutation that occurred more than forty million years ago in our shared primate ancestor, affecting the gene that encodes the L - gulonolactone oxidase (GULO) enzyme.

The loss of function mutation in L - gulonolactone oxidase occurred in the common ancestor to Haplorhini, at least 65 million years ago, so every ancestor since then prevented scurvy with dietary vitamin C from fruits and leafy greens.

In this antioxidant context, it is also worth pointing out the potentially unique relationship between flavonoids and vitamin C. Recent studies have shown the ability of flavonoids to alter transport of vitamin C, as well as to alter function of an enzyme called ascorbate oxidase, which converts vitamin C into a non-vitamin form (monodehydroascorbate).

When cytochrome c - oxidase and NADH are activated by laser light they increase the synthesis of ATP, accelerating cellular function.