Exergonic reactions give off energy. This is because there is enough energy already there to drive the reaction, without requiring any form of extra input (such as ATP)

THIS IS A NEGATIVE DELTA G

These reactions will NOT occur spontaneously. The need energy, such as ATP, to drive it.

THIS IS A POSITIVE DELTA G

• It's Gibbs', or Gibbs' way of measuring free energy
• Delta G 0 prime (wish I could right these out), refers to standard conditions, and what would happen naturally without any outside help
• It's usually compared to the actual delta G of a reaction. LOOK AT THE PICTURE[image]

• The GENERAL process is taking a 6 carbon sugar and burning it for energy, also releasing 6CO₂ out (that stuff we exhale and stuff).
• This is a catabolic process don't forget that or else....
• The cell wants the energy from the C-H bonds (these are full of higher energy electrons)

It is basically the transfer one electrons from one molecule to another within a reaction.

The oxidized molecule loses electrons

The reduced electron gains electrons

They use hydrogen atoms (whole fish electron and proton). AH + B ---> A + BH.

Just like in chemistry when we do a LiAlH₄ reaction, the hydrogen plus TWO electrons (its own and the bond), represented by [H^-] transfers over.

In the case of FADH₂, you get two hydrogen, each with one electron.

COENZYMES. Techinally these aren't enzymes at all but we just call them that cause we're cool and stuff.

The biggest purpose of coenzymes is to accept hydrogen atoms (you need to something to accept these when they fly out of a reaction).

The overall delta G 0 prime = -686 kcal/mole. Naturally, a glucose molecule is burned in just one big step and all almost all the energy is lost as heat, and little is captured as work.

A cell, those cleverl little things, break the process down into 10 smaller steps, maing it easier to capture the energy from each step. Still, most goes off to heat, but they can still capture slightly more.

36. This is about 38% of the glucose's total free energy.

He keeps telling us we don't need ot know exact numbers, but I don't believe it.

• There are 10 whole steps
• The first three use energy to prime the molecule so it can better be burned systematically for energy.
• The middle steps first cleave the originial glucose into two separate molecules, and then use oxidation to not only produce ATP but also reduced coenzymes (2 NADH produced).
• The last steps use coupled reactions to create ATP and pyruvate, to later be used.

• STOP. IT'S HAMMERTIME. Unfortunately the hammertime was a lie, but yes stop. Remember the "waterfall effect" from the cotransporters on test one? Good. Now proceed.
• If you have one reaction that gives off energy and one that requires energy, they can link together. The reaction giving off energy will drive the reaction that requires it.
• IMPORTANT: Take both negative and positive G. If the absolute value of the exergonic reaction is HIGHER than the endergonic, then you are good to go.

Simple my friends, in steps 1, 2 and 3. Or during the priming.

Cell uses energy from ATP ---> ADP (an exergonic, negative G) to drive the creation (an endergonic, pos. G) of a more reactive glucose molecule, fructose 1,6-bisphosphate.

(**HINT, put the bold words together to make a concept**)

Delta G is always assumed under standard conditions. When mass action, occurs, there are no standard conditions. The product of the reaction has a smaller molar concentration, and because of this it is driving the reaction forward. 

I imagine tug of war. And the product keeps "running away" to later parts of the reaction, taking the rope with it. If there is a lot of product, then there will always be some sitting around, not "pulling the rope" as it goes to later parts of the reaction and therefore not causing the reaction to happen at all.

Two membranes! First one is fairly simple, round membrane with large pores in it that allow diffusion of large molecules. Second layer is extremely folded and has many inward things (I forget the name) that increase surface area and what not blah blah blah.

The inside is so thick with proteins that it's basically a gel. IT'S NEGATIVE RELATIVE TO THE OUTSIDE!!!

• Gram negative bacteria, mostly because of they possess a giant protein called porin.
• Theory claims that long time ago a eukaryote engulfed a prokaryote and they started living symbiotically.
• They have their own fussion and fission cycles, so can split and replicate as much as needed when there is an increased need for mitochondria.

Basically mitochondria are like the cells most badass component. If I die and come back as a cell component, I'd be this.

• Pyruvate hits a the pyruvate dehydrogenase complex, with breaks it down into an acetyl group, with a biproduct of CO2. This dehydrogenase is MASSIVE, containing over 60 subunits.
• Then, it attaches to conenzyme A, creating Acetyal CoA. During this process, a reduction occurs, creating one NADH per pyruvate, or 2 NADH per glucose (2 pyruvate per glucose).

It is a series of coupled reactions (much like glycolysis) that work to reduce coenzymes and further break down the acetyl group. By the time it is done, pyruvate is completely oxidized and the original carbon atoms from glucose are being exhaled as CO2.

The useful energy from the glucose is now within the reduced coenzymes.

• 3 molecules of NADH and one molecule of FADH2.
• It also produces one molecule of GTP (which can also be used as energy) and two molecules of CO2.

• It is a way to get electrons from the cytoplasm into the matrix, through a series of linked reactions.
• IT IS NOT A TRANSPORTER. It takes a reduced NADH and oxidizes it. These electrons go through the shuttle and reduce and NAD+ inside of the matrix. The NADH/NAD+ molecules STAY IN THERE RESPECTIVE LOCATIONS
• It does this so that the oxidized NAD+ in the cytoplasm can GO BACK and help with glycolysis

It's basically a naturally occurring form of recycling within a cell (that's how I like to think of it).

• The Malate Shuttle creates 2NADH per glycolysis (remember in step 6 there are two NADH reduced b/c of the cleaved molecule??).
• All in all, we have 10 NADH (4 x 2 from the Kreb's cycle and acetyl, plus 2 from the Malate shuttle) and 2 FADH2 (one for each turn of Kreb's).

• One NADH can make 3
• One FADH2 can make 2
• This difference exists because the oxidation of NADH gives off more energy. Along with that, the cell can better harness this energy.
• GTP. With the 2 from the Kreb's cycle, it's equivalent about two ATP.

• It works by successively move electrons to successively weaker reducing agents.
• Everytime this happens, the change in redox potential gives off neg. delta G. This energy does NOT MAKE ATP, but it is what's used to MOVE THE PROTONS.
• A bunch of complexes and more coenzymes that can move electrons around, each time capturing a little of their energy (kinda like how glycolysis is broken down into little steps to better capture energy).

It's basically exactly the same (conceptually) as everything we've done so far...

1. When electrons go into complex I, it uses some of it's energy to pump an H+ through and then transfer it to coenzyme 2. The energy needed to send this transport is gained by some of the reactions within coenzyme I with the e-.
2. Coenzyme 2 goes to complex III, where again the same thing occurs, pumping a proton and the e- is transferred to cytochrome c (which has an iron binding site so it can bind electrons).
3. Complex IV does literally the exact same thing, passing the e- on to lower energy states, and taking the energy to pump a proton.
4. At the end, the e- has so little energy it is not useful anymore, and is picked up by an O atom. If O was not there (hence needing O2 for mitochondria to work), the e- would get stuck in complex IV, stopping the whole process.

When an HO free radical is produced. These are no bueno because they will take electrons off of ANYTHING (proteins, nucleic acids, etc.) which can change shape and function.

Lou Gerig's disease.

If too much happens in one cell, just kill it.

• FADH2 requies a different complex to oxidize it- complex II
• Complex II takes the electron out of FADH2 and puts it into coenzyme 2, sending it to complex III, then following the same path as NADH.
• However, complex II does not have the ability to harness the passing of electrons to a lower state to pump protons!

O for open. L for lose. And T for tight (shit just got awkwardly sexual with this protein).

One head (getting even worse here) has 3 conformations at once (wow). Every time it spins, conformations change (damn we lost it).

• O: the open conformation has a very low but higher affinity for Pi and ADP than ATP. ATP cannot bind to this AT ALL.
• L: ADP and Pi have a "loose" affinity, but basically same exact thing as O. ADP and pi won't leave once in this and ATP cannot bind AT ALL.
• T: ADP and pi OR ATP CAN ALL BIND TO THIS. When squeezed in this conformation, the reaction from ADP and ATP is at equilibrium and the product will be bouncing back and forth constantly, resulting in a 50/50 of chance of having one or the other.

• Triglycerides. They can be cleaved in halvsies to produce 3 lipid tales and 3 glycerols. Glycerols plus ATP = G3P, so 3 G3P per fat.
• This process skips the first two couple reactions of glycolysis that USE ATP. W/o using these first two steps, you're net gain is 2 ATP higher!

• They go into the beta oxidation cycle/fatty acid cycle!
• You basically oxidize the shit out of them which in turn, at then end, creates acetyl CoA.
• You guessed it, acetyl CoA goes right into the Kreb's cycle in the exact same place and does the exact same thing.
• If needed, you can do the math. But big picture- no matter what you're digesting it all results in reduced coenzymes.

1. Hormonal signaling: basically fat cells along with some other stuff can release hormones that tell you when and when not to eat (very big picture).
2. You can stop the specific process of glycosylation by pumping excess G3P in at step 5 to inhibit mass action and stop the reaction
3. Allosteric Regulators

1. One, I don't know.
2. Two, during steps 1, 3 and 10. Now onto specifics...

• The product has the ability to go back and slow it down! Fancy eh?
• The reaction is sped up by the enzyme hexokinase. The product, glucose-6-phosphate, has a special binding site for hexokinase. It can bind at this site and stop hexokinase. Without hexokinase, not ATP is broken down, so there's no energy and therefore no way to drive the reaction forward.

• Exactly the same as 1.
• However, ATP can also inhibit the pyruvate kinase here as well.
• Either way, both stop pyruvate kinase from making pyruvate, which would stop ATP production.

1. ATP
2. AMP
3. Citric
4. Fructose 2,6-bisphosphate

When you have plenty of energy, ATP and citric are going to be high. When you don't have enough energy, AMP is going to be high. This concept drives the regulation...

• If you have a ton of ATP/citric floating around, there's a greater chance it will bind to phosphofructokinase-1 and slow down its enzimatic action (word is completely made up on my part).
• If you have a ton of AMP floating around, there's a greater chance it'll bind to phosphofructokinase-1 and speed up enzimatic (awesome) activity, giving you more energy.
• Kinda fancy how it all works eh?

• First off it's good to know that this speeds up and not slows down the reaction...
• In step 3, the first molecule, fructose-6-phosphate, can, through a separate enzyme (phosphofructokinase-2) and commas everywhere, make this F26B. Then this F26B can come in and stimulate production.
• But you say how does that help if it need to take away F6B to make it. But just remember this- the benefits greatly outweight the costs. The amount of stimulation this provides the reaction is worth the amount it takes away from F6B.

1. Cotransporters and ATP concentration
2. Uncoupling proteins

• Cotransporters use the energy from one favored gradient to move another thing against an unfavored gradient.
• You need ADP to make ATP in the mitochondria. So...
• The flow of ATP out of the mitochondria to the cytoplasm (favored, going with the gradient) moves ADP into the mitochondria (unfavored, against the gradient).
• If you have lots of energy and ATP in the cytoplasm is high, not as much ATP will go out, give less power to move ADP in. Without ADP on the inside, there is nothing to make ATP with!!! BOOM.

SEALS AND POLAR BEARS AND WALRUSES AND SHIT YEAH ACTIC POLE CRITTERS HAVE THESE!

• Basically these are little things in the membrane between matrix and IM that allow free H+ diffusion back into the matrix.
• It is extremely easy for H+ protons to get through these, so it greatly decreases the amount that go through the BADASS LITTLE ATP SYNTHASE MACHINE!!!! Therefore, ATP production slows.
• They produce a very significant and large amount of heat (which is why all the adorable north pole critters have a lot of them).
• They are made from brown fat