Bacteria, mitochondria and chloroplasts

all use chemiosmosis to generate ATP

Mitochondria contain two membranes and two aqueous compartments
each of which contains a unique set of proteins.
Fig 5.3 p181
Fig 3.27 p113
Fig 5.5 p183


The mitochondrial inner membrane and matrix are the sites of
most reactions involving the oxidation of pyruvate and the coupled synthesis of ATP
Mitochondrial oxidation of pyruvate begins
with the formation of acetyl CoA
The multienzyme complex pyruvate dehydrogenase converts
pyruvate and coenzyme A into CO
2
and acetyl CoA
From glycolysis,
Pyruvate decarboxylase
From oxidation of fatty acids
In mitochondria
Aka TCA, Krebs cycle

Fig 5.6 p185
Tricarboxylic Acid (TCA)
Cycle
Krebs Cycle
Citric acid cycle
A summary of the reactions of
glycolysis and the citric acid cycle
Electron transport and oxidative
phosphorylation
Most of the free energy released during oxidation of glucose
to CO
2
is retained in NADH and FADH
2

During respiration, electrons are released from NADH and
FADH
2
and eventually are transferred to O
2
(forming H
2
O)
The step-by-step transfer of electrons via the electron
transport chain allows the large amount of free energy
produced by the transfer of electrons to O
2
to be released in
small increments
Several electron transport chain components convert these
small increments into a proton and voltage gradient across
the inner membrane
The movement of protons down their electrochemical
gradient drives the synthesis of ATP from ADP and P
i

The stepwise flow of electrons through the electron
transport chain from NADH, succinate, and FADH
2
to 0
2

Reduction
potentials of
electron carriers
favor electron
flow from NADH
to O
2

Fig 5.14 p192
Table 5.1 p190
Electron transport in mitochondria is
coupled to proton translocation
The multiprotein complexes and associated prosthetic
groups of the mitochondrial electron transport chain
The pathway of electron transport and proton
transport in the inner mitochondrial membrane
Fig 5.17 p194
NADH FAD
1
2
_
O2
H O 2
FMN
Fe-S
Fe-S
Fe-S
Q
Matrix
Inner
Memb
Complex
I
Complex
II
Complex
III
Complex
IV
NADH FAD
1
2
_
O2
H O 2
FMN
Fe-S
Fe-S
Fe-S
Q
Matrix
Inner
Memb
Complex
I
Complex
II
Complex
III
Complex
IV
H
+
H
+
H
+
Fig 5.10 p187
Fig 5.12 p191
Coenzyme Q is the only electron carrier that
is not a protein-bound prosthetic group
Three-dimensional structures of some iron-
sulfur clusters in electron-transporting proteins
Fig 5.13 p192
Oxidation of reduced cytochrome c by cytochrome c
oxidase is coupled to proton transport
Coupling of H
+
pumping and O
2
reduction
by cytochrome c oxidase
Fig 5.18 p195
Uncoupler
2,4-dinitrophenol (DNP)

Thermogenin
Natural uncoupler
Brown adipose tissue
ATP Synthase
Fig 5.22 p199
Fig 5.3 p181
ATP synthase comprises a proton channel
(F
0
) and ATPase (F
1
)
Fig 5.24 p200
Fig 5.24 p200
Fig 5.29 p204
Proton Diffusion
ATP Synthase F1 Head
Fig 5.26 p202
The F
0
F
1
complex harnesses the proton-
motive force to power ATP synthesis
Binding Change Mechanism
Fig 5.27 p203
Demonstration that the subunit of F
0
rotates relative to the
()
3
hexamer in an energy-requiring step
Fig 5.28 p203
Fig 5.30 p205
Summary
Specific uptake-targeting sequences in newly made
proteins are recognized by different organelles
Overview of sorting of nuclear-
encoded proteins in eukaryotic cells
Most mitochondrial proteins are synthesized as
precursors containing uptake-targeting sequences
Uptake-targeting sequences of imported
mitochondrial proteins
Fig 8.47 p317
Fig 8.47 p317
Mitochondria and chloroplasts
Contain their own
prokaryote-like genomes and
ribosomes
Likely evolved from
bacteria that were
endocytosed
(ingested)

Endosymbiont
Hypothesis
Fig 1 p27
Fig 1 p27
Similarities to Bacteria
a) DNA is circular
b) Size of ribosome 70s
c) antibiotic sensitivity (inhibit protein synthesis)
Chloramphenicol inhibits Mito + Bacteria but not
cytosolic ribosmes
Cycloheximide inhibits cytosolic ribosmes but not
Mito + Bacterail ribosomes
d) Replication
Mitochondria and Bacteria
Fig 5.2 p180