Fosforilación oxidativa

Chapter 19, pp. 659-690

Ilona I. Concha, Ph.D.

6 carbon

C6H12O6 + 6 O2 → 6 CO2 + 6 H2O

2 x 3 carbon

2 CO2

2 x 2 carbon

The carbon is
already converted to
2 x 2 CO2
CO2.
What is left is
electrons in the
form of NADH and
FADH2.
NAD+/NADH

Coenzyme Q
FAD/FADH2

Hemes
Iron-Sulfur Centers
 Determining the sequence of electron carriers
using inhibitors of electron transfer

Those that are reduced are blue. Those that stay oxidized are pink
Complex I: NADH to Coenzyme Q
Complex II: Succinate to Coenzyme Q
Complex III:Coenzyme Q to Cytochrome c
Complex IV: Cytochrome c to O2

SDH is on the
matrix side of
the IMS
SDH
Coenzyme Q
 Complex III structure
(half of the functional dimer)
Cytochrome c
 Core of Complex IV is
comprised of 3 subunits

Subunit II
CuA (2 Cu)

Subunit III
CuB

Subunit I
heme a, heme a3, and CuB
O2 + 4 H+ + 4 cyt c (Fe2+) → 2 H2O + 4 cyt c (Fe3+)
Proton-motive force
 Coupling of electron
transfer and ATP
synthesis in isolated
mitochondria

Dinitrophenol causes
dissipation of the protn
gradient and thus uncouples.
Inhibits ATP Synthase
Model of
ATP
Synthase
complex
ADP
ATP
ADP

ATP
Binding-change
model for ATP
synthase
Shuttle systems are required for mitochondrial oxidation of cytosolic NADH
 Uncoupled
mitochondria
in brown fat
produce heat
Regulation of the ATP-
producing pathways