Molecular Mechanism of ATP synthesis

[q0L0b]

nice animation but adding some narration would be very helpful....thanks.

[TheGrotesqueReality]

Sound Sound......

[JTS11d6]

This is the shit, to think that this is the source of energy for all biological reactions.

[DreamsofMajesty]

scribd (dot) com/nb812

[BlackyJerome]

Very nice and demonstrative!! but this is ATP-synthetis backward right? and I couldn't identify the neon green atom, what is it?Thanks^^

[wolfgangouille]

@BlackyJerome It is Mg2+

[TheFluorineMartyr]

Isn't that beautiful?

[CookieMcWeaksauce]

Hehe, yeah. I was realllly confused until I realized a Pi group was leaving - the reaction is runnign backwards. Misleading video title is...misleading.

[CurtisVector]

If this really is depicting the action of ATP synthase, then it's showing the chemical reaction going backwards. I'll explain the reaction taking place first how it is depicted (as if it were the hydrolysis of ATP to form ADP and Pi, moving forward in time), and then I'll explain the reverse reaction (as if it were depicting the synthesis of ATP backwards in time, though my explanation will move forwards in time). Since these comments have a character limit, I'll do it in a series of replies.

[CurtisVector]

First, ATP can be seen entering the active site with its triphosphate moeity coordinated to a magnesium ion, as is typical for cytoplasmic ATP. No hydrogen atoms or double bonds are shown, their presence is implied. The complex then changes conformation to accommodate the entering ATP, and several arginine residues (positively charged, hydrogen bond donors) can be seen hydrogen bonding to the phosphates (negatively charged, hydrogen bond acceptors (via oxygen atoms)).

[CurtisVector]

The conformation continues to change as the reaction progresses. The incoming white ball is the nucleophilic water molecule in an Sn2 reaction with the gamma phosphate. It can be seen hydrogen bonded to serine, glutamic acid, and arginine residues. After the reaction occurs, the substrates leave the active site, and the conformation returns to its native state. I forgot to mention earlier that you can see phenylalanine and tyrosine residues forming Van der Waals interactions with adenine.

[CurtisVector]

The second half of the animation is showing the same thing from a different perspective.

If you were to visualize this reaction in reverse, the beta phosphate of ADP would become the nucleophile (via an oxygen atom) and the water molecule would become the leaving group of the Sn2 reaction.

Sorry if that was unclear. I'm not trying to show off by using chemistry/biochemistry jargon, just trying to be as unambiguous as possible.

[mutatron]

Looks like some ATP went in and some ADP came out. This thing needs a voice over.

[hajuch0]

can someone explain to me what everything is ?? i have a presentation to make on March 20th !! please i need help... i dont understand :(

[theinsane102]

lol, should of looke don wikki, it explains it in laymen's terms

[smokedog77]

it would be nice if there was sound to this video describing what everything is

[xgalba01]

That yellow thing is mitochondria? It doesn't look easy this Crebs cycle.

[nschmid]

No the yellow thing is the ATP synthase protein. Is hasn't much todo with the Crebs cycle. The crebs cycle is involved in carbohydrate breakdown and produces mainly NADH. The NADH is used to pump protons over the inner membrane of the mitochondria. This is the respiratory chain. This electrochemical gradient then drives the ATP synthase and ATP is formed from ADP and phosphate.

[xgalba01]

Thank you for your great explanation. I watched more videos on this stuff and now I understand what you wrote. Before it was Chinese for me

[Fomelogo]

That's great. It's the best video i've ever seen about this.

I'm a biochemestry student and it really helped me on learning

THANKS

THANKS

THANKS

[teocoroi]

suuuper tare animatia! suuper tare microbiologia!

[am03ph]

hmm..How was this animation generated, VMD?

[soulsora]

muy buena animacion, sole le falta un poco d audio. sigan haciendo mas forfavor