Reduction of NAD+

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Reduction of NAD+

Post by illuminada » Sun Jun 12, 2011 5:18 am


It would be wonderful if somebody could do a little explaining. Even if they only know a tiny bit =).

Ok, so I know that NAD+ is reduced to NADH by the action of dehydrogenases. Which means means that it gains electrons (2 electrons I think) and a hydrogen.

I don't really know what a dehydrogenase is only that it sounds like an enzyme that would take hydrogens away from other things. Which is fine because obviously to give NAD+ a hydrogen, it would have had to take it away from something.

But then there is these things called hydrogenases (I think) and that sounds like an enzyme that would give something a hydrogen, however it would first have to take the hydrogen from something else, right?

So my questions are; what is the difference between a dehydrogenase and a hydrogenase? And why/how do the dehydrogenases reduce NAD+, converting it into NADH?

Thank you very much for taking the time to read my question. =) I appreciate any and all help given to me, even if its just an idea you have and you arent sure its completely right. =)

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Inland Taipan
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Post by JackBean » Tue Jun 14, 2011 8:32 am

You need to understand the difference between substrate and cofactor. The NAD+/NADH is cofactor.
The dehydrogenases take hydrogens from substrates and put them to the cofactors, which can be subsequently reoxidized either with the same enzyme (typically flavin coenzymes) or in other enzyme (typically nicotinamide cofactors)

Cis or trans? That's what matters.

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