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deoxy-form: oxy-form:
five-coordinate six-coordinate
hs Fe(II) diamagnetic
4 unpaired [hs Fe(II) + O2
electrons ls Fe(III)-O2(-.)]
Fe(II) is out of Fe(III) is in the
porphyrin ring plane of the
by ~0.5 Å towards porphyrin ring.
histidine.
Crystal-Field Splitting Diagrams
dx2-y2, dz2
dx2-y2
dz2
dxy
P-450 enzymes are generally membrane bound and have been found in plants,
animals, yeasts, and bacteria. The best characterized P-450 enzyme is the soluble
camphor-metabolizing P450-CAM isolated from Pseudomna putida.
Cytochrome P450: hydroxylation (monooxygenase)
Chem. Rev.
1987, 87, 1255-1276
Catalytic Cycle of Cytochrome P450
Chem. Rev.
1987, 87, 1255-1276
Science 1988,
240, 433-439
Peroxidase
(2 7 8 2)
oxidizing substrates
with simultaneous
reduction of
H202 to H20
Catalase
(2 7 2)
H202 to
02 and H20
Summary reaction:
The complex is a large lipoprotein composed of several metal prosthetic sites and 13
protein subunits in mammals. In mammals, ten subunits are nuclear in origin and
three are synthesized mitochondrially. The complex contains two hemes, the ''a'' and
''a3'' hemes, and two copper centers, the CuA and CuB centers. In fact, the heme ''a3''
and CuB are a binuclear center that is the site of oxygen reduction. The mechanism
of action of this large complex is still an active research topic.
Respiration: Aerobic Metabolism
Oxidation of food generates electrons
- 0.32 V +0.82 V
NAD+ + H+ + 2e- NADH
O2 + 4H+ + 4e- 2H2O
Cytochrome c Oxidase
Heme a
CuB
a3-CuB
Chem. Rev. 1980, 90, 1247–1260
Chem. Rev. 2017, 117, 3717−3797
Chem. Rev. 2018, 118, 2491−2553
Chem. Rev. 2018, 118, 10840−11022