Tag: biochemistry

Folate Deficiency Vs Vitamin B12 Deficiency

Check out my brand new “Electrolytes” course at https://www.medicosisperfectionalis.com/products/course/electrolytes/ and use the PROMO code: ELECTROLYTES50 to get a 50% discount. ► Right Now! You can get access to all my hand-written hematology video notes (the notes that I use on my videos) on Patreon…There is a direct link through which you can view, download, print and enjoy! Go to https://www.patreon.com/medicosis I have discussed Folate deficiency as well as Vitamin B12 deficiency before in separate videos.

This is a series on “anemia”, go to my playlist named: “hematology/oncology”.

RDW is elevated in both Vitamin B12 deficiency as well as in folate deficiency.

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If you would like a good pharmacology textbook, try Lippincott illustrated: https://goo.gl/PYEUP2

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Vitamin C | Masterclass With Masterjohn 1.5

The role of vitamin C in the antioxidant defense system, its interaction with smoking and vitamin E, and how its chemistry, biochemistry, and physiology can help us understand its distribution and stability in natural foods.

Glutathione Reductase, B Vitamins, and Glucose | Masterclass With Masterjohn 1.10

Glucose is the ultimate antioxidant. In this lesson, we look at how energy is transferred from glucose to the antioxidant system using the help of B vitamins, and discuss why a large range of carbohydrate intakes is likely to provide equivalent support to this pathway.

Lexicon of Biochemical Reactions: Vitamin B6 / PLP

MIT 5.07SC Biological Chemistry, Fall 2013
View the complete course: http://ocw.mit.edu/5-07SCF13
Instructor: JoAnne Stubbe

This video focuses on another cofactor: Vitamin B6 (Pyridoxine). This is the cofactor you use whenever you want to metabolize amino acids. We use amino acids to make fats or sugars depending on what the environment is telling us we need to do.

License: Creative Commons BY-NC-SA
More information at http://ocw.mit.edu/terms
More courses at http://ocw.mit.edu

Electron Transport Chain ETC Made Easy

Electron Transport Chain ETC Made Easy

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GLYCOLYSIS : https://www.youtube.com/watch?v=8qij1m7XUhk

KREBS CYCLE : https://www.youtube.com/watch?v=ubzw64PQPqM&t=181s

Beta oxidation: https://www.youtube.com/watch?v=__jS-pjzb5k&t=5s

An electron transport chain (ETC) is a series of complexes that transfer electrons from electron donors to electron acceptors via redox (both reduction and oxidation occurring simultaneously) reactions, and couples this electron transfer with the transfer of protons (H+ ions) across a membrane. This creates an electrochemical proton gradient that drives the synthesis of adenosine triphosphate (ATP), a molecule that stores energy chemically in the form of highly strained bonds. The molecules of the chain include peptides, enzymes (which are proteins or protein complexes), and others. The final acceptor of electrons in the electron transport chain during aerobic respiration is molecular oxygen although a variety of acceptors other than oxygen such as sulfate exist in anaerobic respiration.

In chloroplasts, light drives the conversion of water to oxygen and NADP+ to NADPH with transfer of H+ ions across chloroplast membranes. In mitochondria, it is the conversion of oxygen to water, NADH to NAD+ and succinate to fumarate that are required to generate the proton gradient.
Complex I
In Complex I (NADH:ubiquinone oxidoreductase, NADH-CoQ reductase, or NADH dehydrogenase; EC, two electrons are removed from NADH and ultimately transferred to a lipid-soluble carrier, ubiquinone (Q). The reduced product, ubiquinol (QH2), freely diffuses within the membrane, and Complex I translocates four protons (H+) across the membrane, thus producing a proton gradient. Complex I is one of the main sites at which premature electron leakage to oxygen occurs, thus being one of the main sites of production of superoxide.
The pathway of electrons is as follows:

NADH is oxidized to NAD+, by reducing Flavin mononucleotide to FMNH2 in one two-electron step. FMNH2 is then oxidized in two one-electron steps, through a semiquinone intermediate. Each electron thus transfers from the FMNH2 to an Fe-S cluster, from the Fe-S cluster to ubiquinone (Q). Transfer of the first electron results in the free-radical (semiquinone) form of Q, and transfer of the second electron reduces the semiquinone form to the ubiquinol form, QH2. During this process, four protons are translocated from the mitochondrial matrix to the intermembrane space. [4] As the electrons become continuously oxidized and reduced throughout the complex an electron current is produced along the 180 Angstrom width of the complex within the membrane. This current powers the active transport of four protons to the intermembrane space per two electrons from NADH.
Complex II
In Complex II (succinate dehydrogenase or succinate-CoQ reductase; EC additional electrons are delivered into the quinone pool (Q) originating from succinate and transferred (via flavin adenine dinucleotide (FAD)) to Q. Complex II consists of four protein subunits: succinate dehydrogenase, (SDHA); succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial, (SDHB); succinate dehydrogenase complex subunit C, (SDHC) and succinate dehydrogenase complex, subunit D, (SDHD). Other electron donors (e.g., fatty acids and glycerol 3-phosphate) also direct electrons into Q (via FAD). Complex 2 is a parallel electron transport pathway to complex 1, but unlike complex 1, no protons are transported to the intermembrane space in this pathway. Therefore, the pathway through complex 2 contributes less energy to the overall electron transport chain process.

Complex III
In Complex III (cytochrome bc1 complex or CoQH2-cytochrome c reductase; EC, the Q-cycle contributes to the proton gradient by an asymmetric absorption/release of protons. Two electrons are removed from QH2 at the QO site and sequentially transferred to two molecules of cytochrome c, a water-soluble electron carrier located within the intermembrane space. The two other electrons sequentially pass across the protein to the Qi site where the quinone part of ubiquinone is reduced to quinol. A proton gradient is formed by one quinol (2H+2e-) oxidations at the Qo site to form one quinone (2H+2e-) at the Qi site. (in total four protons are translocated: two protons reduce quinone to quinol and two protons are released from two ubiquinol molecules).

QH2 + 2 cytochrome c (FeIII) + 2 H+in → Q + 2 cytochrome c (FeII) + 4 H+out
When electron transfer is reduced (by a high membrane potential or respiratory inhibitors such as antimycin A), Complex III may leak electrons to molecular oxygen, resulting in superoxide formation.

CHECK OUT NEWEST VIDEO: “Nucleic acids – DNA and RNA structure ”


Niacin, Part 1: What It Is and Why You Need It | Mastering Nutrition #60

Niacin is vitamin B3. You use it to make NAD, the ultimate anti-aging molecule that repairs your DNA and lengthens your telomeres, and the most foundational molecule in our entire system of energy metabolism.

It is especially important to protecting your mind, your skin, and your gut.

You use it to release all your neurotransmitters. This is why depression sets in as the earliest sign of deficiency and why, when it gets bad enough, it leads to suicidality or schizophrenia-like psychosis.

You use constantly it to repair the microscopic damage done to your skin every time you step out into the sunlight. This is why red, inflamed skin appears on the backs of your hands or on your face when you’re deficient, but only if you get outdoors a lot.

You use it to fuel the rapid turnover of cells in your intestines (the cells that absorb the nutrients in our food are replaced every 2-3 days!), and to repair those cells from the constant barrage of insults they face (think of everything those cells *don’t* let in our body 💩and the fact that *they* need to stare all that stuff down!) This is why deficiency will give you diarrhea and make you deficient in lots of other nutrients.

You use it for lots of other things too, like participating with riboflavin to make the methyl group of methylfolate and recycle glutathione, the master antioxidant of the cell. You use it to recycle vitamin K, to support detoxification in the liver, and to synthesize cholesterol, fatty acids, neurotransmitters and nucleotides.

Who needs more? We all do!

Why? Because just aging alone depletes niacin and getting sick or developing diseases as we age depletes it all the more. Niacin repairs damage, so the more damage we face the more we consume.

In fact, this is why many people are taking supplements like nicotinamide riboside (NR) or nicotinamide mononucleotide (NMN), to slow the onset of aging, or to age more gracefully. Some people are even injected NAD!

But should we be?

And what about the dark side of niacin? We all know the flush — the redness and itching that accompanies high-dose niacin that people take to lower cholesterol. At high doses, niacin can even damage the liver. How? By sapping methyl groups. Sapping methyl groups can give you liver failure when it’s *really* bad, but sapping them just a little can leave you feeling weak, emotionally stuck, or tied up in a mental funk.

In this two-part podcast series, Alex Leaf and I tackle all of these questions. Click the link to listen to part 1, where we teach you what niacin is and why you need it.

In part 2, two weeks from today, we’ll cover how to get niacin in foods, blood tests, and supplements.

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Pentose Phosphate Enzymes, ATP, and B Vitamins | Masterclass With Masterjohn 1.11

Today’s lesson covers the contribution of two critical enzymes — glucose 6-phosphate dehydrogenase and transketolase — to antioxidant defense, and takes a deeper look at the roles of thiamin, niacin, and riboflavin.