0% found this document useful (0 votes)
3 views20 pages

1730483423_Lecture 2 Oxadative phosphorylation _ETC_

Download as pdf or txt
Download as pdf or txt
Download as pdf or txt
You are on page 1/ 20

Oxidative Phosphorylation /

Electron Transport Chain /


Respiratory Chain

EL-RAZI UNIVERSITY
2ND YR / 1ST SEM.

FahadSabir©2023
Body Fuels (Energy Rich Molecules)
• In order to survive and perform body vital functions, all
cells constantly require chemical energy, mainly derived
from ATP.

• Cells produce ATP (The Energy Currency) by two main


mechanisms:
1. Substrate Level Phosphorylation .
2. Oxidative Phosphorylation (Electron Transport Chain).
Oxidation/Reduction
• In oxidative Phosphorylation, ATP produced
as follow:
• In the cell , energy-rich molecules such as glucose,
fatty acids (body fuels) are utilized constantly in
organized sequence of reactions (catabolic
pathways) involve oxidation reactions.

• Most of energy released from these (oxidation


reactions) captured by energy-rich Reduced
Coenzymes:
• NAD+  NADH + H+
• FAD  FADH2.
Oxidation/Reduction

NAD: Nicotinamide Adenine Dinucleotide, from vitamin B3 Niacin.


FAD: Flavin Adenine Dinucleotide, from vitamin B2 Riboflavin.
Electron Carriers in Inner Mitochondrial Membrane
• In mitochondria, the reduced
coenzyme Re-Oxidized and donates a
pair of electrons to molecular Oxygen
to form water.
• (NADH + H+) + O (1/2O)  NAD+ + H2O.
• (FADH2) + O (1/2O)  FAD + H2O

• Before the pair of electrons received


by oxygen, they transported through a
set of electron carriers located in the
Inner Mitochondrial Membrane in a
process called Electron Transport
Chain.
Components of the ETC
Complex I (NADH Dehydrogenase)

Location: Impeded in inner Mitochondrial Membrane


Structure: Enzyme (Dehydrogenase) + Coenzyme (FMN)
Function: Transfer 2 electrons [as H2] from NADH+H+ to FMN which
becomes FMNH2
Components of the ETC
Complex II (Succinate Dehydrogenase)

Location: Mitochondrial Matrix (TCA Cycle).


Structure: Enzyme.
Function: Transfer 2 electrons (As H2) from FADH to Coenzyme Q.
Components of the ETC
Coenzyme Q (Ubiquinone)

 Location: Mobile component in inner mitochondrial membrane


 Structure: Quinone Derivative, small, (similar to Vitamin K).
 Function: Transfer the 2 electrons (H2) from complex I (FMNH2) and
complex II (FADH2) to Complex 3.
Components of the ETC
Complex III: Cytochrome bc1

• Location: Impeded in inner Mitochondrial Membrane.


• Structure: Cytochrome contains Heme group with Fe3+ (Hb).
• Function: Transfer the 2 electrons from Coenzyme Q to Cyt C.
Components of the ETC
Cyt C: Cytochrome C

• Location: Mobile component in inner mitochondrial membrane.


• Structure: Cytochrome protein contains Heme group with Fe3+ (Hb).
• Function: Transfer 2 electrons from complex III to complex IV.
Components of the ETC
Complex IV: Cytochrome C oxidase (cytochrome a + a3)

• Location: Impeded in inner Mitochondrial Membrane.


• Structure: Cytochrome contains Heme group with Fe3+ (Hb).
• Function: Transfer the 2 electrons from Cyt c to 1/2O2 to give H2O.
Components of the ETC
Complex V: (ATP Synthase)

 Location: Impeded in inner Mitochondrial Membrane


 Structure: Protein (Enzyme) with two domains (Fo and F1).
 Function: ATP synthesis from ADP.
ATP Synthesis: Chemiosmotic Hypothesis
 While electrons transported across inner mitochondrial membrane,
protons (H+) pumped out from the matrix to the intermembrane space
at Complexes I, III, and IV.
ATP Synthesis: Chemiosmotic Hypothesis
 This process creates an electrical and pH gradient (more positive
charges and lower pH on outside of the membrane than inside.
 The energy generated by this proton gradient is sufficient to drive ATP
synthesis.
ATP Synthesis: Chemiosmotic Hypothesis
 Protons pumped outside the inner mitochondrial membrane, they
reenter the matrix by passing through a channel in domain (Fo) of
Complex V.
 This drives the rotation of Fo and dissipating the pH and electrical
gradients.
ATP Synthesis: Chemiosmotic Hypothesis
 Fo rotation causes conformational changes in the F1 domain that allow
it to bind ADP + Pi, phosphorylation, and release ATP.
 This is called Chemiosmotic Hypothesis.
Oligomycin
 Oligomycin (drug) binds to the Fo domain of ATP synthase, closing the
H+ channel, preventing reentry of protons into the mitochondrial matrix,
and thus preventing phosphorylation of ADP to ATP.
More Figures for ETC
More Figures for ETC
More Figures for ETC

You might also like