Ubiquinone (Q) is reduced by four ways;

a. By the oxidation of NADH in complex I
b. Electrons from succinate pass through a flavoprotein with the cofactor FAD and several Fe-S
centers (in Complex II) on the way to Q
c. Glycerol 3-phosphate donates electrons to a flavoprotein (glycerol 3-phosphate dehydrogenase)
on the outer face of the inner mitochondrial membrane, from which they pass to Q.
d. Acyl-CoA dehydrogenase (the first enzyme of oxidation) transfers electrons to electron-
transferring flavoprotein (ETF), from which they pass to Q via ETF

TLS Online TPP Program

#Id: 5883

#Unit 3. Fundamental Processes

Semiconservative replication

DNA repair reaction

TLS Online TPP Program

#Id: 5884

#Unit 3. Fundamental Processes

All prokaryotic and eukaryotic DNA polymerases share the same fundamental type of synthetic activity -an antiparallel synthesis from 5’ to 3’ from a template that is 3’ to 5’. This means adding nucleotides one at a time to a 3’–OH end.

TLS Online TPP Program

#Id: 5885

#Unit 3. Fundamental Processes

Hydrolysis of pyrophosphate is the driving force for DNA synthesis

TLS Online TPP Program

#Id: 5886

#Unit 3. Fundamental Processes

The DNA polymerase monitors the ability of the incoming nucleotide to form an A:T or G:C base pair, rather than detecting the exact nucleotide that enters the active site in a DNA polymerase with significantly reduced discrimination

between dNTPs and rNTPs.

TLS Online TPP Program

#Id: 5887

#Unit 3. Fundamental Processes

Only when a correct base pair is formed are the 3’-OH of the primer and the a-phosphate of the incoming nucleoside triphosphate in the optimum position for catalysis to occur.

TLS Online TPP Program

#Id: 5888

#Unit 3. Fundamental Processes

Incorrect base pairing leads to dramatically lower rates of nucleotide addition as a result of a catalytically unfavorable alignment of these substrates. This is an example of kinetic proofreading, in which an enzyme favors catalysis using one of several possible substrates by dramatically increasing the rate of bond formation only when the correct substrate is present.