#cytochrome chain

[biology-geology-beaches-india]

The Science Research Diaries of S. Sunkavally. Page 169.

[tenth-sentence]

Cyanide inhibits cytochrome c oxidase in the mitochondria, which blocks the electron transport chain.

"Plant Physiology and Development" int'l 6e - Taiz, L., Zeiger, E., Møller, I.M., Murphy, A.

[tommies-stinky-paws]

I wanna start a picrew chain because I've finally found one that has everything I've been looking for >:3

no guidelines, no nothing, just make what you look like or your ideal self :3

here the link

and here's me :DDD

tagging (/nf): @cytochrome-sea @sunfl0wersapphic @sparks-chaotic-cove @sunnymellow09 @disappointedcreeper @rivals-legacy

(hey mooties sorry for the tag on my alt lol)

[gray-matter-in-a-teacup]

Cyanide Poison

Let's start by understanding exactly how cyanide kills you. In simple terms, cyanide prevents cells from using oxygen to make energy molecules.

The cyanide ion, CN-, binds to the iron atom in cytochrome C oxidase in the mitochondria of cells. It acts as an irreversible enzyme inhibitor, preventing cytochrome C oxidase from doing its job, which is to transport electrons to oxygen in the electron transport chain of aerobic cellular respiration. Now unable to use oxygen, the mitochondria can't produce the energy carrier adenosine triphosphate (ATP). Tissues that require this form of energy, such as heart, muscle cells, and nerve cells, quickly expend all their energy and start to die. When a large enough number of critical cells die, you expire as well. Death usually results from respiratory or heart failure.

Immediate aymptoms include headaches, nausea and vomiting, dizziness, lack of coordination, and rapid heart rate. Long exposure symptoms include unconsciousness, convulsions, respiratory failure, coma and death.

A person exposed to cyanide may have cherry-red skin from high oxygen levels, or dark blue coloring, from Prussian blue (iron-binding to the cyanide ion). In addition to this, skin and body fluids may give off an almond odor.

The antidotes for cyanide include sodium nitrite, hydroxocobalamin, and sodium thiosulfate.

A high dose of inhaled cyanide is lethal too quickly for any treatment to take effect, but ingested cyanide or lower doses of inhaled cyanide may be countered by administering antidotes that detoxify cyanide or bind to it. For example, hydroxocobalamin, natural vitamin B12, reacts with cyanide to form cyanocobalamin, which leaves the body in urine.

These antidotes are administrated via injection, or IV infusion.

Cyanide is actually a lot more common than you'd think. It's in pesticides, fumigants, plastics, and electroplating, among other things. However, not all cyanide are so poisonous. Sodium cyanide (NaCN), potassium cyanide (KCN), hydrogen cyanide (HCN), and cyanogen chloride (CNCl) are lethal, but thousands of compounds called nitriles contain the cyanide group, yet aren't as toxic. They still aren't terribly good for you, so I wouldn't go around ingesting other cyanide compounds, but they're not quite as dangerous as the lethal kind.

Thank you for reading, have a lovely day :)

[science-lover33]

Unraveling the Tapestry of Cellular Energy: A Comprehensive Voyage through the Electron Transport Chain 🧬⚙️

Prepare for a deep dive into the labyrinthine pathways of the Electron Transport Chain (ETC), where molecular machinations weave the intricate tapestry of cellular respiration. In this odyssey, we'll navigate the complexities with surgical precision, leaving no nuance unexplored.

1. Prelude at Complex I (NADH Dehydrogenase):

The ETC's overture commences at Complex I, where NADH, a product of glycolysis and the Krebs cycle, surrenders its high-energy electrons. Traverse the serpentine route of flavin mononucleotide (FMN) and a succession of iron-sulfur clusters, witnessing the orchestrated dance that propels electrons toward the enigmatic ubiquinone (Q).

2. Interlude with Succinate (Complex II - Succinate Dehydrogenase):

As the symphony progresses, Complex II takes the stage with succinate as its protagonist. Succinate dehydrogenase, fueled by succinate from the Krebs cycle, orchestrates a parallel electron flow. Behold the ballet of electrons navigating iron-sulfur clusters and flavin adenine dinucleotide (FAD), converging upon ubiquinone (Q) in a seamless choreography.

3. Cytochrome Waltz (Complex III - Cytochrome bc1 Complex):

The narrative crescendos at Complex III, the cytochrome bc1 complex, where Q takes center stage. Through a series of mesmerizing redox reactions, Q gracefully shuttles electrons to cytochrome c. This transient dancer becomes the ethereal messenger, ferrying electrons with finesse towards the climactic rendezvous at Complex IV.

4. Grand Finale with Complex IV (Cytochrome c Oxidase):

In the climactic finale, Complex IV, personified by cytochrome c oxidase, awaits the electron ensemble. Watch as electrons, guided by a cascade of copper and iron centers, engage in a captivating pas de deux with molecular oxygen. Witness the alchemical metamorphosis as oxygen is humbly transmuted into water, marking the zenith of our electron saga.

5. Proton Symphony and ATP Synthesis:

Simultaneously, the proton symphony unfolds as protons, displaced during electron transit, accumulate in the intermembrane space. This sets the stage for a grand energy transfer. The finale crescendos with protons flowing back through ATP synthase, a molecular turbine, culminating in the synthesis of ATP—the lifeblood of cellular energy currency.

References:

1. Alberts, B., Johnson, A., Lewis, J., Raff, M., Roberts, K., & Walter, P. (2014). Molecular Biology of the Cell (6th ed.). Garland Science.

2. Nelson, D. L., Cox, M. M. (2017). Lehninger Principles of Biochemistry (7th ed.). W.H. Freeman and Company.

3. Berg, J. M., Tymoczko, J. L., Gatto, G. J. S., & Stryer, L. (2019). Biochemistry (8th ed.). W.H. Freeman and Company.

[electricfox]

CALLING ALL FURRIES, THERIANS AND OTHER ART DORKS

I found a cute f2u pride base by Antynah on Toyhouse and I think we should all get together this pride month and draw our ocs, fursonas, personas, or therotypes using this base! ^_^

Pride base with Trans + Queer alts

Have fun everybody!!! Make a chain :D

Tagging: @legosetboyfriend @canines-crown @xemmez @doggycorspe @cytochrome-sea @fluffywolfboyy

[save-the-villainous-cat]

ermmie wormiee....can you explain how light dependant reactions work I'm genuinely kinda lost on that part of AP Bio like everything else makes sense but unit 3 (enzymes photosynthesis and cellular resp) is genuinely my OP

Ok, so I don’t know how much you have to know so let’s just get into it. It’s not that hard once you get it.

Also please keep in mind that I studied all of this in German so I’m sorry if some things are worded weirdly.

So, there are two photosystems (PSII and PSI) in plants. As you can see in this pic, the whole reaction starts with PSII, not PSI — that’s because PSI was discovered first. (But that’s not really important.)

Photosystems are able to absorb photons (that come from the light) and produce a high energy electron! As you can see in this pic, PSII absorbs the photon, creates a high energy electron and sends it through an electron transport chain (Plastoquinone - that’s a molecule btw) to the Cytochrome b6f complex and from there to PSI.

PSII uses water as an electron donor! That is very important because that’s how oxygen gets created as a by-product.

(sciencefacts.net)

PSI absorbs the photon again and produces another high energy electron which converts NADP+ to NADPH.

The big question is: how does the plant create ATP now?

That happens through non-cyclic photophosphorylation. See all those H+ protons? Whereas there is a bunch inside the thylakoid lumen, there isn’t much in the stroma.

That leads to a concentration compensation. So all those little protons that have been produced during the reaction actually go through the ATP-synthase into the stroma. Thus, the ATP-synthase creates ATP!

I also had to remember this, I don’t know if you do but if you have any questions about it, feel free to ask:

(istudy.pk)

All you need to know is basically:

Light hits PSII. Light = energy. PSII needs energy to turn electron (water = electron donor) into a high energy electron. High energy electron travels. H+ protons get produced during reactions. PSI needs energy. High energy electron converts NADP+ to NADPH (we need that for our Calvin cycle later). Bunch of protons travel through ATP-synthase —> we have ATP now!!!

I hope this makes somewhat sense. As I’ve mentioned, I had to remember all of this in German so yeah it might be a bit messy. If there’s anything unclear, feel free to send another ask!

[anulithots]

go ahead & talk about caspases

So I'm using this article for my ramblings (I annotated it and went feral): Paradoxical roles of caspase-3 in regulating cell survival, proliferation, and tumorigenesis - PubMed (nih.gov)

The research article, and how to storyfy it

SO the crux of this article - being called the ‘paradoxical functions of caspases’ and all - is that capase-3’s cause cell proliferation and cleavage in more than just apoptosis, implying that their function is widespread throughout the cell.

Now that sounded formal. Here’s how I’ll story-fy it. So Cassiah the Caspase-3 wants to not be attached to the world because their purpose is to destroy it. If death lies at the end of this then why suffer the pain of wanting something from this? However, because of thrill life offered after the Caspase-9 first awoke them, they want their life to mean something. They want their life to be so full of meaning and fulfillment at every moment that death wouldn’t matter much anyways.

So with the dual purposes of caspase-3’s, the question of whether Cassiah is meant to cause apoptosis or something else is uncertain. What Cassiah knows is that they want to fulfil their itches and urges to kill/cleave proteins

(We’ll have cleaving be a sort of ‘blood transformation’. So they must be cut in a certain way… similar to those blood sigil things)

They know that cleaving other proteins would give their buzzing energy in a search for more a rest, that would be the moment they finally are content.

Now the Caspase-9 that awoke Cassiah believes that Cassiah must meet the expectations of their purpose. Don’t ask questions. If Cassiah is meant to cause the death of the cell then so be it. Attempting to avoid this fate would only cause more heartache. ‘This is real. If you get caught in dreams of grandeur, as you, as a caspase… then I can only wish that you realize the truth before the end.’

Casapse-9/intrinsic pathway activation (this one involves cytochrome-c from the mitochondria, fun fun):

In essence, external growth factors cease, the outside world doesn’t want anything from this cell anymore. Stressors such as ‘viral infections, hypoxia, hyperthermia, oxidative stress, and intrinsically detected stress signals resulting from exposure to toxic chemical or radiation exposure’. So the outside world is cut off, something on the inside is wrong.

As far as signaling goes, I imagine something akin to carrier pigeons? … I still have to figure out what sort of style of world this is, but honestly I’m leaning more and more towards ‘biology first then the rest melds around that’. So either more sentient ‘carrier pigeon’ types or little floating things (magic sparkles of sorts) that land upon certain proteins or other receptors that cause some sort of shift or change. In this case. Stress signals. They cause certain alarms to go off, such as this pathway. So is everyone aware that the world might end? Yes and no. It depends on who you are, and given that cell signaling is complex, I imagine that everyone has their own idea/awareness of what is going on. If a protein goes about their day and recognizes a little signal floating around among the slew, the hustle and bustle of things floating around, then that might be a cause for concern.

From here the signals cause the mitochondrial membrane to be more permeable.

Now for membranes, their built of this ‘ramen type thing’ (similar to how people build all sorts of things with ramen… but more magical and fancy and such )

… so we’re going with magical absurdism here.

Anywho, so the phospholipid bilayer… would probably look around the same? Heads facing the outside, so it’s bumpy, along with the inside looking like stringy ramen. So that becomes looser…

and things

begin

to

leak.

SUCH AS CYTOCHROME C!

I forget what this was used for in cellular respiration because…. cellular respiration… I’d need to review some of that. If I remember correctly, it was part of oxidative phosphorylation… the electron transport chain?

So that starts bleeding into the surrounding space, which forms a apoptosomal complex that includes caspase-9.

Storyfying wise - Caspase-9 has lied dormant in this biomechanical machine (sci-fi is slowly but surely becoming more intriguing to me), waking rarely, always a hush hush if they do. For that, everyone knows (at least everyone in the know knows) that could end in disaster.

So the cytochrome c causes that biomechanical mass to awaken, a sore and tired and… dread-filled caspase-9 within.

(We’re going to be looser with personalities needing backstories to explain every facet here for my own sanity)

This caspase-9 then - still shaking off the aches of dormancy - awakens their ‘younger sibling who will cause the end of the world’

And here, they feel a touch of pity. It’s not fair. Really. It’s not fair yet this is what it is, how the Caspase-9 wishes it didn’t have to do this, but the universe itself is against any rebellion, and they don’t want any pain unto themself.

Caspase-3s’s are these little caspase-3 assassins that kill off caspase-3’s. The way this whole thing with all the opposing signals works here is that… this is an entire world here. IN order to have the ‘right thing’ done, there must be conflict, someone who wins out in the end, it’s a fragile balance.

So the Caspase-9… now here’s the part where I’m still figuring it out… it’s okay but it could be better…

The caspase-9 manages to save only one of the caspase-3’s from the caspase-3s, Cassiah, who does seem a little shaken from the whole ordeal, and a little hesitant to follow their whole purpose, they don’t leave immediately… In fact, they aren’t really shaken, they are thrilled.

Oh. What an issue.

The Caspase-9 easily forgets the other caspase-3’s, and this more than anything frightens Cassiah, while the Caspase-9 tells them that this, whatever this is, they just escaped with their lives here. They could’ve easily been killed as well, then the Caspase-9 would need other caspase-3’s to replace Cassiah. THe world doesn’t care. There’s no solace outside of the promise of being useful. Any attempt otherwise ends in heartache.

Now here Cassiah wonders what would’ve happened if they had died right then, before they got the chance to fully experience something, it wouldn’t have been such a pain then. It would’ve been like sleeping more after a brief interruption.

Does the world care? Is there a meaning to this?

Perhaps not.

But they want a meaning to this. To their life. They want to live and savor every moment of it so even if they had died in the next, they could’ve died fulfilled, full, with a meaning to even death.

So Casaiah’s really fighting against their own desire to live well with the promise of a meaningless but purposeful existence, one that is guaranteed not to hurt, to be satisfying in the end, as long as they don’t resist.

(Sigh I won’t really get this until I start writing Cassiah prose)

the dual purpose of caspase-3

Caspase-3’s cleave other proteins, inhibitors, and such. Again, I imagine this would involve a high-stakes kidnapping a blood-sigil-type-thing where Cassiah cuts just so for the protein to change purpose/activate or deactivate.

Now part of what they do is cut inhibitors, for instance, they cut an inhibitor that keeps DNA from fragmenting. An inhibitor inhibits caspase-activated DNAse, once Caspse-3 removed the inhibitor, caspase-activated DNAse condenses and cleaves DNA at ‘interneucleosomal linker sites between nucleosomes’

OTHER RESULTS: so, because of Caspase-3’s other downstream targets ‘phosphatidylserine from the inner layer of the plasma membrane’ leaks from the membrane to the outside of the cell. It binds to the cell surface and calls phagocytes to the cell to consume it. This is a preliminary sign of apoptosis

~Storyfying this - So BLOOD SIGILS CARVED INTO THE FLESH.

ANd I doubt articles will have the specific targets because cell signaling is…. complicated so say the least, so I have some creative liberty here.

In Cassiah’s little adventures around the cell, they have sudden thoughts to do the deed. They will have to kidnap them, take them somewhere private and carve the sigil into flesh, they will change shape as a result.

As far as their morals go with this, they don’t want to be forgotten, so they are perfectly fine with doing the deed itself (what’s more memorable than a life-changing event?) however apoptosis is possible. Apoptosis, in which everything will be forgotten. It wouldn’t have mattered if Cassiah existed or not, their life wouldn’t have meant anything, and that scares them more than anything .

So despite their desire to do the whole blood sigil thing, they avoid it, they even save others for the sake of avoiding apoptosis.

other things:

Caspase-3 activity causes ‘nonautomatous and cell autonomous (or direct) mechanisms of initiation and execution’

nonautomatous refers to the adjacent cells proliferating to replace the apoptotic cell

Caspase-3 activates pathways, starts pathways, interferes with pathways that can lead to tissue growth and wound healing. (nonautonomous) Which is not so fun for tumors and such…

cell autonomous refers to the apoptotic cell itself and how Capase-3

capase-3’s are also known to cleave substrates during the M to G1 transition step in mitosis even when apoptosis will not occur

“This has been explained by caspse-3 mediating the cleavage of p21 (the cyclin-dependent kinase [CDK] inhibitor) at its C terminus, thereby disrupting the ability of p21 to interact with proliferating cell nuclear antigen (PCNA) leading to cell cycle inhibition” ←- basically Caspase-3 can start the cell cycle which IS CRAZY TO ME AAAAAAAAAAAAAAAAAAAAAA

SO STORY WISE

There will definitely be an episode in which Cassiah finds out that they could be involved in mitosis rather than apoptosis. So they spend time around cyclin-dependent kinases for the day and see if they feel any ‘blood sigil urges’

The nonautomnous parts of this are fun, but since they are outside the scope of the cell, I am unsure of if I can include them, but it would be fun if I could because it’s peak angst. (being replaced and such.)

ALSO ALSO

procaspase-3 affects MITOCHONDRIAL REGULATION

“In this case, the suppression of Caspase-3 expression led to mitochondrial dysfunction, accumulation of damaged mitochondria, and downregulation of key transcriptional activators of mitochondrial biogenesis”

PEOPLE POEPLE SKJDSKLFJKDLSJ AAAAAAAAAAAa

SO BASICALLY

I was wrong that procaspases float in a void and are deactivated. They actually work to regulate the mitochondria. KLJDFKJDSLKF but here’s the thing. I built Cassiah’s character off of existing first as floating within the void. If that’s not the case, then I need to change thier entire character to fit around this more. Hopefully it will be easier… maybe…. sighhhh

Now as fun as researching about caspases has been, it’s really for the purpose of character building, now I want to look more into diving deeper on all the AP bio topics and fully fleshing out this world and the themes.

ANd now I also have to rework Cassiah’s character after finding out about this mitochrondria thing…. sigh sigh I should’ve finished the article before I started.

ERM... yes. OKAY SO biology taglist... you do not have to read all this.

The lovely biology taglist: @vamp4ever @bonesbeetle @neurospicy-salsa @sea-dwelling-wizard

[blueoaknx]

The Story of Mitochondria: Evolution, Function, and Molecular Machinery

Mitochondria are double-membraned organelles that play an essential role in cellular bioenergetics and various metabolic pathways. Known primarily as the “powerhouses of the cell,” mitochondria generate most of the cell’s adenosine triphosphate (ATP) through oxidative phosphorylation (OXPHOS). Beyond energy production, these organelles regulate several crucial functions, including apoptosis, calcium signaling, and reactive oxygen species (ROS) management. This article delves into the technical aspects of mitochondrial evolution, structure, functions, and their involvement in disease, illuminating why these unique organelles are pivotal to cellular health.

Evolutionary Origins: The Endosymbiotic Theory and Genome Reduction

Mitochondria originated from an ancient symbiotic event approximately 1.5–2 billion years ago, when an ancestral eukaryotic cell engulfed a free-living, aerobic bacterium. This theory, known as the endosymbiotic theory, was proposed by biologist Lynn Margulis in the 1960s and has been widely substantiated by evidence from molecular biology and genetics. The engulfed bacterium eventually became an organelle within the host cell, providing a selective advantage by supplying ATP through aerobic respiration.

Over evolutionary time, mitochondrial DNA (mtDNA) underwent significant gene reduction, as many genes were either lost or transferred to the nuclear genome. The modern human mitochondrial genome is compact, with only 37 genes remaining, encoding 13 proteins essential for oxidative phosphorylation, 22 transfer RNAs (tRNAs), and 2 ribosomal RNAs (rRNAs). Most of the proteins required for mitochondrial function are now encoded by nuclear DNA and imported into the mitochondria via translocases and specialized import machinery. This gene reduction reflects a co-evolution of mitochondria with the eukaryotic host, solidifying their role as a semi-autonomous organelle within eukaryotic cells.

Structure and Compartments of Mitochondria

Mitochondria have a highly specialized structure, featuring a double membrane that divides them into distinct compartments: the outer membrane, intermembrane space, inner membrane, and matrix. This compartmentalization enables spatial separation of various metabolic processes and facilitates the generation of a proton gradient necessary for ATP synthesis.

Outer Membrane: The outer mitochondrial membrane contains porins—integral membrane proteins that allow the free diffusion of molecules up to 5 kDa. This membrane also contains enzymes involved in lipid synthesis and oxidation. The voltage-dependent anion channel (VDAC) is a key protein of the outer membrane, mediating metabolite exchange and regulating ion permeability.

Intermembrane Space: The intermembrane space lies between the outer and inner membranes and contains enzymes involved in processes such as nucleotide phosphorylation. It also plays a critical role in the apoptosis pathway, as cytochrome c and other pro-apoptotic factors are released into this space before initiating the apoptotic cascade.

Inner Membrane: The inner membrane is rich in proteins and contains the electron transport chain (ETC) complexes, which carry out oxidative phosphorylation. This membrane is impermeable to most ions and molecules, ensuring that the proton gradient established by the ETC is maintained. The inner membrane’s distinctive folds, known as cristae, increase the surface area available for oxidative phosphorylation and house the complexes I-IV, ATP synthase, and various other transport proteins.

Matrix: The mitochondrial matrix is the innermost compartment and contains enzymes for the tricarboxylic acid (TCA) cycle, mtDNA, ribosomes, and tRNAs. The matrix environment is essential for mitochondrial gene expression and also serves as a site for other metabolic reactions, such as fatty acid oxidation and amino acid synthesis.

Oxidative Phosphorylation and ATP Production

The primary function of mitochondria is to produce ATP through the process of oxidative phosphorylation, which occurs in the inner membrane and involves the electron transport chain (ETC) and ATP synthase.

Electron Transport Chain (ETC): The ETC comprises four protein complexes (Complexes I-IV) that facilitate the transfer of electrons from electron carriers NADH and FADH₂ to molecular oxygen (O₂). Complex I (NADH dehydrogenase) and Complex II (succinate dehydrogenase) initiate electron transfer, followed by Complex III (cytochrome bc₁ complex) and Complex IV (cytochrome c oxidase). As electrons pass through these complexes, protons (H⁺) are pumped from the matrix to the intermembrane space, creating an electrochemical gradient across the inner membrane.

ATP Synthase: The proton gradient generated by the ETC drives the synthesis of ATP via ATP synthase (Complex V), a molecular motor that converts ADP and inorganic phosphate (Pi) into ATP. As protons flow back into the matrix through ATP synthase, the energy released is used to phosphorylate ADP. This process, chemiosmosis, is central to ATP production and is the primary source of energy in eukaryotic cells.

Mitochondrial DNA and Genetic Regulation

Mitochondrial DNA (mtDNA) encodes a small but essential portion of the proteins required for mitochondrial function. Mitochondrial genes are transcribed within the matrix by mitochondrial RNA polymerase, and translation occurs on specialized mitochondrial ribosomes that resemble bacterial ribosomes. Despite their independence in certain functions, mitochondria rely heavily on nuclear-encoded proteins, which are imported into the organelle through translocase complexes (TOM and TIM) on the outer and inner membranes, respectively.

Notably, mtDNA has a high mutation rate due to limited DNA repair mechanisms and exposure to reactive oxygen species (ROS) generated during oxidative phosphorylation. Mutations in mtDNA can lead to defects in ETC complexes, impairing ATP production and resulting in a range of mitochondrial diseases.

Regulatory Roles Beyond Energy Production

In addition to ATP synthesis, mitochondria regulate several essential cellular processes, including:

Apoptosis: Mitochondria play a central role in programmed cell death (apoptosis) through the release of cytochrome c and other pro-apoptotic factors from the intermembrane space. Once in the cytoplasm, cytochrome c binds to Apaf-1, leading to caspase activation and cell death.

Calcium Signaling: Mitochondria act as calcium reservoirs, modulating intracellular calcium levels by sequestering and releasing Ca²⁺. The mitochondrial calcium uniporter (MCU) imports Ca²⁺ into the matrix, influencing metabolic activity by activating TCA cycle enzymes.

Reactive Oxygen Species (ROS) Production: Mitochondria are the primary source of ROS in cells, especially superoxide (O₂•⁻), which is produced during electron transfer in the ETC. Mitochondria contain antioxidant enzymes like superoxide dismutase (SOD) and glutathione peroxidase to neutralize ROS. However, excessive ROS can lead to oxidative stress, damaging cellular structures, mtDNA, and contributing to aging and degenerative diseases.

Mitochondrial Dysfunction and Disease

Mitochondrial dysfunction can result from mtDNA mutations, nuclear DNA mutations, or environmental factors that impair the ETC and ATP production. This dysfunction is implicated in numerous disorders:

Mitochondrial Myopathies: These disorders affect skeletal muscle, leading to muscle weakness and fatigue. Mutations in mtDNA or nuclear DNA affecting ETC proteins often underlie these diseases.

Neurodegenerative Diseases: Impaired mitochondrial function is associated with neurodegenerative conditions like Parkinson’s, Alzheimer’s, and Huntington’s diseases. Mitochondrial dysfunction in neurons leads to reduced ATP production, increased oxidative stress, and apoptosis, all contributing to neurodegeneration.

Cardiovascular Diseases and Aging: Age-related decline in mitochondrial function and mtDNA mutations contribute to reduced ATP production and increased ROS. This decline is associated with sarcopenia, cognitive aging, and increased susceptibility to cardiovascular diseases.

Advances in Mitochondrial Research

Research on mitochondrial therapeutics is advancing, focusing on treatments that can enhance mitochondrial function or compensate for defects. Approaches such as mitochondrial replacement therapy (MRT), antioxidant therapy, and targeted gene editing are under investigation. Lifestyle factors, including diet and exercise, have also been shown to positively influence mitochondrial function, providing non-invasive strategies to support mitochondrial health.

Conclusion

The technical story of mitochondria encompasses their unique evolutionary origin, complex structure, and multifaceted roles in cellular homeostasis. Far beyond simple energy producers, mitochondria are integral to cellular regulation, signal transduction, and apoptosis. As research progresses, understanding the intricate molecular machinery and regulation of mitochondria holds promise for developing therapies for mitochondrial diseases and conditions linked to aging.

[copperproducts]

The Science Behind Copper: Why It's Essential for Your Health

Copper, a trace mineral found in various foods and essential for the body's overall function, plays a significant role in maintaining health. Despite being required in small amounts, copper is indispensable for numerous physiological processes, including energy production, connective tissue formation, brain function, and the immune system. Understanding the science behind copper and its health benefits sheds light on why this mineral is vital for our well-being.

The Role of Copper in the Body

Copper is a cofactor for several enzymes known as cuproenzymes. These enzymes facilitate various biochemical reactions in the body. One of the critical functions of copper is its role in energy production. Copper is a component of cytochrome c oxidase, an enzyme in the mitochondria responsible for the final step in the electron transport chain, which generates ATP, the cell's primary energy currency.

Additionally, copper is crucial for the formation and maintenance of connective tissues. Lysyl oxidase, a copper-dependent enzyme, is essential for the cross-linking of collagen and elastin, two proteins that provide strength and elasticity to connective tissues like skin, bones, and blood vessels. This process is vital for wound healing, maintaining the integrity of blood vessels, and ensuring the strength of bones and cartilage.

Copper and the Nervous System

The nervous system relies heavily on copper for optimal function. Copper is involved in the synthesis of neurotransmitters, the chemical messengers that transmit signals between nerve cells. Dopamine-beta-hydroxylase, an enzyme that converts dopamine to norepinephrine, requires copper to function correctly. Norepinephrine is a neurotransmitter essential for mood regulation, alertness, and stress response.

Moreover, copper contributes to the formation and maintenance of myelin, the protective sheath around nerve fibers that ensures efficient transmission of nerve impulses. Copper deficiency can lead to neurological issues, including impaired motor coordination and cognitive function.

Copper's Role in the Immune System

A well-functioning immune system is crucial for defending the body against infections and diseases. Copper enhances the immune system by stimulating the production and activity of immune cells. It helps in the production of white blood cells, including neutrophils and macrophages, which are essential for phagocytosis—the process of engulfing and destroying pathogens.

Furthermore, copper possesses antimicrobial properties. It can kill or inhibit the growth of bacteria, viruses, and fungi, making it an essential element for maintaining immune health and preventing infections.

Sources of Copper and Daily Requirements

Copper is naturally present in a variety of foods. Good dietary sources include shellfish, seeds and nuts, whole grains, dark leafy greens, and organ meats. For most people, a balanced diet provides sufficient copper to meet daily needs. The recommended daily allowance (RDA) for copper varies by age, sex, and life stage, but for adults, it is approximately 900 micrograms per day.

Risks of Copper Deficiency and Toxicity

While copper deficiency is rare, it can occur, especially in individuals with certain genetic disorders, malabsorption issues, or those who rely on parenteral nutrition. Symptoms of deficiency include anemia, weakened immune response, neurological problems, and cardiovascular issues.

On the other hand, excessive copper intake can lead to toxicity, resulting in symptoms like abdominal pain, nausea, vomiting, and, in severe cases, liver damage and kidney failure. Therefore, it is essential to maintain a balanced intake of copper through diet and avoid excessive supplementation unless prescribed by a healthcare provider.

Conclusion

Copper's role in energy production, connective tissue formation, nervous system function, and immune health highlights its importance as an essential mineral. Ensuring adequate copper intake through a balanced diet can support these vital processes and improve overall health and well-being. Understanding the science behind copper underscores why this trace mineral is indispensable for maintaining a healthy body.

[tenth-sentence]

The individual electron transport proteins are organized into four transmembrane multiprotein complexes (identified by roman numerals I through IV), all of which are localized in the inner mitochondrial membrane.

"Plant Physiology and Development" int'l 6e - Taiz, L., Zeiger, E., Møller, I.M., Murphy, A.

[ujjawalachemical]

Ujjawala Ferrous

Ferrous Sulphate (as Fe) 19% Ujjawala Ferrous contains Iron (as Fe) 19% and Sulphur (as S) 10.5%. Iron plays vital role in photosynthesis and breakdown of carbohydrates. Iron play a significant role in various physiological and biochemical pathways in plants. It severs as components of many vital enzymes such as cytochromes of the electron transport chain, and it is thus required for a wide range of biological function in plants. It ensures normal growth of crops & high-quality yields and is suitable for all crops. Deficiency Symptoms: Iron deficiency results in yellowing between the leaf veins of young leaves. Browning of leaf edges also occurs in acid- loving plants. Dosage: Soil Application: Apply 10 kg of Ujjawala Ferrous per acre for all crops.

[downincmi]

Sodium Cyanide Market Trends: Insights and Forecasts

Introduction Sodium cyanide is an odorless chemical compound with the formula NaCN. It is a white, water-soluble solid. NaCN has a wide range of industrial and other applications, but it is also notoriously toxic and has sometimes been used for suicide or murder. Let's explore some key facts about this dangerous chemical compound. Chemical Properties and Structure Sodium cyanide has the chemical formula NaCN and a molar mass of 49.01 g/mol. It dissociates in water to give hydroxide (NaOH) and cyanide (CN-) ions. The cyanide ion is linear with carbon and nitrogen separated by a triple bond. It is this CN- ion that is primarily responsible for NaCN 's high toxicity. NaCN is a white solid that melts at 563°C to give a colorless liquid. It is highly soluble in water. Toxicity and Mode of Action Cyanide is an inhibitor of cytochrome c oxidase, an important enzyme in the mitochondrial electron transport chain. By blocking this enzyme, cyanide essentially prevents aerobic respiration from taking place at the cellular level. This leads to a rapid depletion of oxygen to tissues and ultimately causes death due to hypoxia at the tissue and organ level. The lethal dose of NaCN for adult humans is reported to be 200-300 mg. However, as little as 1-5 grams can prove fatal. The primary symptoms of cyanide poisoning include headaches, dizziness, confusion, convulsions and cardiac arrest. Death by cyanide poisoning usually occurs within minutes to an hour. There is no antidote for cyanide poisoning. Treatment focuses on supportive measures in a hospital environment along with use of antidotes like sodium thiosulfate or dicobalt edetate to combat the effects of cyanide. Industrial Uses Despite its obvious toxicity, NaCN has many beneficial industrial applications primarily due to its ability to dissolve minerals containing precious metals like gold and silver. It is widely used for extraction of these metals via cyanidation process in mining operations. In this process, an aqueous solution of NaCN is used to leach gold from minerals into the water to facilitate separation and recovery of gold. NaCN is also used in some cleaning and metal surface treatment applications. Other uses include: Production of nylon - Sodium cyanide serves as an intermediate for adiponitrile, which is further used to make nylon 6,6. Case hardening - It is used in metallurgy for case hardening of steels to increase wear resistance and hardness. Alkylation - In organic chemistry, NaCN acts as an alkylating agent in production of compounds like acrylonitrile. Accidental and Intentional Poisonings There have been many accidental and intentional deaths reported due to sodium cyanide poisoning over the years. Accidental cases may occur due to occupational exposure in industries using cyanide or due to consumption of cyanide-containing products mistaken as food. Intentional poisonings with cyanide have been reported in cases of suicide or murder. Some high-profile murder cases have involved the use of NaCN by the perpetrator. Given the acute toxicity of cyanide ions, even small amounts ingested intentionally can prove rapidly lethal. Proper safety precautions are a must for any activities involving this deadly chemical salt. Regulation and Safe Handling Considering the high human toxicity of NaCN, it is designated as a schedule 2 substance under the Chemical Weapons Convention. Many countries have strict regulations governing its manufacture, transportation, storage and industrial usage. Workers directly handling NaCN must be properly trained in safety procedures like wearing recommended personal protective equipment. Leakage of cyanide solutions into the environment must also be prevented to avoid toxicity to other organisms. Overall, given the risks involved, sodium cyanide requires controlled and regulated use with utmost precautions taken at all stages to prevent accidental poisonings.

[yeast-papers]

Biogenesis of cytochromes c and c1 in the electron transport chain of malaria parasites

BioRxiv: http://dlvr.it/T2C3pD

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I would also add that there is such thing as synonymous substitution - a type of mutations, that doesn't change the resulting protein. That can happen because the genetic code is redundant - meaning that most amino acids (the basic blocks from which proteins are made) can be encoded in a number of different three letter combos.

The fact that such "silent" mutations occur allows us to identify different species by analysing the sequence of such common proteins you are talking about. Added benefit is - because the proteins are so similar, we can use the same primer (the thingy that basically encodes which part of genome we want to analyse (you can read more on wiki in the linked article, I won't go into detail here) to analyse biological material from a vast number of organisms (as opposed to species specific markers, which, you guessed it, work only on one or several closely related species).

For example, In our latest work we used a fragment of a cytochrome b protein to differentiate between wolves and golden jackals. The fragment analyzed is about 350 bp (base pairs (letters)) long and has several mutations (letter changes) specific to each species. But the protein that both fragments make are identical.

I'm sorry for a bit of a rumble - I slept like 7 hours in past two days. But I hope you now know a bit more about the fascinating subject of genetics:)

this might be a stupid question, but if theres a protein that multiple organisms need, wouldn't the a t g c genetic code for it be the same for different species? or at least closely related species? so theoretically some prompts/sequences should have multiple fitting organisms or closest fitting organisms

(i know it isn't this simple, but im wondering what the exact reason it doesn't work like that is, or what im missing)

not a stupid question, i'll try to answer it to the best of my understanding, but if anyone has anything to add, please do.

put shortly: you're right! if multiple organisms need a certain protein, the code in their DNA is generally the same in that region.

from a genetics perspective, all organisms are actually extremely similar. i'm sure you've heard that we humans share more than half our genetic information with bananas and such.

this is just a factor of how evolution works. every so often, a mutation occurs in an organism's genome, which has a chance to increase the fitness of that organism, which allows it to have more offspring, which changes the mix of alleles in the population. and this is how we get different species of things.

but, because we all share a common ancestor from a long, long, long, long time ago, we do maintain some similarities, especially in regions that code for things essential to life.

those regions where things are *different* is where we're able to tell one species from another, differentiating moths from trees and such. but, overall, all living organisms have a whole lot in common.

[avantibodyus]

What Should You Know About Red Light Therapy Weight Loss?

Numerous studies have shown that red light treatment, a non-invasive method of low-level laser therapy, can aid in fat loss. While Red Light Body Contouring is not a magic bullet for weight reduction on its own, it has been used successfully by the biohacking community as a supplement to healthy eating and regular exercise to help people shed excess pounds more quickly.

Red light therapy is defined as.

Red light or Body Sculpting Treatmentsis a subset of LLLT that employs the application of bioactive visible and infrared light wavelengths to the affected area. Commonly used photon frequencies include the red end of the visible spectrum (630–660 nm) and the near infrared end (850 nm).

Red light therapy or Body Sculpting Non Surgicalimproves adenosine triphosphate (ATP) production by increasing the availability of oxygen at the fourth step of electron chain transport, when cytochrome c-oxidase is used. Then, localized fat reduction and improved body contouring are possible thanks to adenosine triphosphate.

Some research suggests that Red Light Therapy for Weight Losscan help the body get rid of excess fat by reducing fat cells and then releasing them through the body's natural waste elimination systems. The body's fat cell count drops as a result.

A clinical dermatologist can-do red-light treatment in the comfort of your own home or at a spa. Cost-effective and convenient, Red Light Therapy for Inflammationat home allow you to reap the weight loss advantages of LLLT without leaving the ease of your own home. Studies have revealed that red light treatment can aid with weight loss.

Red light therapy: any risks?

Although red light therapy has been demonstrated to be safe in separate trials, it is better to err on the side of caution. Before beginning a course of red-light therapy, it is wise to consult with your doctor.

A light exposure test should be done before beginning regular use of red-light treatment. This method entails illuminating a small patch of skin with the device's red and infrared lights to see if a reaction occurs.

Red light treatment, whether used at house or in a health club, has been shown in trials to have no serious adverse effects.

Is It Appropriate to Invest in Red Light Therapy?

Red Light Therapy Weight Loss will not be effective unless other crucial lifestyle parameters are also drastically improved. Maintaining a healthy body requires a commitment to both regular exercise and a well-rounded, nutritional diet. Fat loss is increased when combined with red light therapy compared to when either method is used alone.

As a non-invasive method of reducing fat and reshaping the physique, red light therapy has many advantages.

Red light therapy, when combined with a healthy diet and regular exercise, has been shown to be an effective, non-invasive method of accelerating weight loss. Because of the lack of serious safety issues, red light therapy is a great addition to your weight loss arsenal.

Waist, thigh, and hip circumference can all be significantly reduced with regular red light therapy sessions lasting only twenty minutes.