[BIOCHEMISTRY I] Module No.

BIOLOGIC OXIDATION #3.2

Dr. Raymond Oliver A. Cruz September 14, 2016
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Movement of e is from lower to higher potential
Outline
I. Oxidation and Reduction • Oxygen/Water is the final electron acceptor in electron
II. Free Energy Change transport chain
III.Redox Potential • Oxygen/Water is the most probably to receive electrons
IV. Oxidoreductases because of high affinity
A. Types
1. Oxidase
• Cytochrome Oxidase IV. OXIDOREDUCTASES
• Xanthine Oxidase
2. Dehydrogenase • Enzymes involved in oxidation and reduction
• Alcohol and Aldehyde Dehydrogenase • Classified into 4 groups: oxidases, dehydronegases,
• Cythochrome
hydroperoxidases, and oxygenases
• Other Dehydrogenases Depend on Flavin Nucleotide
3. Hydroperoxidase
• Peroxidase
 Glutathione Peroxidase 1. Oxidase
• Catalase
4. Oxygenase • Catalyze the removal of hydrogen from a substrate
• Dioxygenase • Use oxygen as hydrogen acceptor
 Homogentisate Dioxygenase • They form water or hydrogen peroxide as a reaction
 3-Hydroxyanthranilate Dioxygenase product
 L-tryptophan Dioxygenase
• Monooxygenase
 Cytochromes P450
V. Superoxide Dismutase (SOD)
Legend:
Black- Powerpoint
Red- Book
Blue- Audio Recording • Uricase (urate oxidase) catalyzes the following overall
I. OXIDATION AND REDUCTION reaction:

• Oxidation is defined as the removal of electrons
• Reduction is defined as the gain of electrons
II. FREE ENERGY CHANGE
• Can be denoted by the tendency to donate and accept
0´
electrons (like ΔG )
• This is known as the Redox Potential (E´0), or Reduction
Potential
III. REDOX POTENTIAL
• Ability to donate or accept electrons
• The tendency of a chemical to acquire electrons and
thereby be reduced
• The more positive the potential, the greater the species'
affinity for electrons and tendency to be reduced.
• Measured in Volts (V)
• Defined relative to the Standard Hydrogen Electrode (SHE),
arbitrarily given potential of 0.00 volts
• A reduction potential is measured in volts (V) and is defined
relative to the standard hydrogen electrode (SHE), which is
arbitrarily given a potential of 0.00 volts
•
0
Standard reduction potential (E ), is measured under
standard conditions: 25°C, a 1M concentration for each ion
participating in the reaction, a partial pressure of 1 atm for
each gas that is part of the reaction, and metals in their pure
state (Normal Atmospheric Pressure at sea level: 760mm)
• For biologic systems, the redox potential (E΄0) is normally
expressed at pH 7.0 at which pH the electrode potential of the
hydrogen electrode is -0.42 volts
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REDOX POTENTIALS (predict e flow)
• This reaction represents the termination of purine catabolism
in all mammals excluding man, higher apes and the
Dalmatian dog (uricase is absent in these organisms)
1.1 Cytochrome Oxidase
• Final acceptor of electrons before it is pass on oxygen
• Also called cytochrome a3
• More correctly termed cytochrome aa3 since nalaman na yung
heme a3 combines with heme a para maform yung enzyme
complex
• It is a hemoprotein like myoglobin and hemoglobin
• Also contains 2 atoms of copper associated with its 2 heme
molecules
• Terminal component of the respiratory chain found in
mitochondria
• Final electron acceptor is oxygen
• Poisoned by CO, Cyanide, H2S
Poisonous because it neutralizes the
cytochrome oxidase
• If it’s blocked the electrons will not be passed to oxygen and
it will stop the electron transport chain causing unabling it to
form ATP by oxidative phosphorylation thereby preventing
cellular respiration
1.2 Xanthine Oxidase
• Contains molybdenum
• Converts purine base to uric acid
• Important in uricotelic animals (birds, lizards)

SYSTEM E΄0 VOLTS

+
H /H2 -0.42
NAD+/NADH -0.32
Lipoate; ox/red -0.29 2. Dehydrogenase
Acetoacetate/3- -0.27
hydroxybutyrate • Cannot use oxygen as hydrogen acceptor
Pyruvate/Lactate -0.19 • 2 Main Functions:
Oxaloacetate/Malate -0.17 o Transfer of hydrogen from 1 substrate to another in
Fumarate/Succinate +0.03 a coupled oxidation-reduction reaction. It enables 1
Cytochrome b; Fe3+/Fe2+ +0.08
substrate to be oxidized at the expense of another
Ubiquinone; ox/red +0.10
o Component in the respiratory chain of electron
Cytochrome c1; Fe3+/Fe2+ +0.22
Cytochrome a; Fe3+/Fe2+ +0.29 transport from substrate to oxygen
Oxygen/Water +0.82

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[Biochemistry] [Biologic Oxidation] Module 2, Lecture 3

• Contains Selenium as prosthetic group

• Catalyzes the destruction of H2O2 and lipid peroxidases by
converting reduced glutathione to its oxidized form
• Protects membrane lipids and hemoglobin against oxidation
by peroxides

• Glutathione is not only a whitening agent but also a anti-

oxidant

2.1 Alcohol and Aldehyde Dehydrogenase

• Enzymes in mammalian liver

• Contains molybdenum and nonheme iron

3.2 Catalase

• Uses hydrogen peroxide as electron donor and electron

acceptor
• A hemoprotein containing 4 heme groups which can act as a
peroxidase
• Destroys H2O2 formed by the action of oxidases
2H2O2  2H2O + O2
• Peroxisomes are rich in oxidase and catalase
2.2 Cytochromes
• Fastest enzyme reaction known
• Iron-containing hemoproteins • It can be found in the blood, bone marrow, mucous
membrane, kidney & liver.
• All dehydrogenases except cytochrome oxidase
• Electron carriers in respiratory chain
• Also found in endoplasmic reticulum (cytochrome P450) 4. Oxygenase

2.3 Other Dehydrogenases Depend on Flavin Nucleotides • Catalyze the direct transfer and incorporation of oxygen into a
substrate molecule in 2 steps:
• FADH2 is also important because it can be a source of energy 1. Oxygen is bound to the enzyme at the active site
for the cell 2. The bound oxygen is reduced or transferred to the substrate

4.1 Dioxygenase

• Incorporate both atoms of molecular oxygen into the

substrate
• Examples:
1. Homogentisate dioxygenase (liver)
2. 3-hydroxyanthranilate dioxygenase (liver)
3. L-tryptophan dioxygenase
1 and 2 contain iron; 3 utilizes heme
3. Hydroperoxidases
4.1a Homogentisate Dioxygenase
• Use hydrogen peroxide or an organic peroxide as substrate
• Protect the body against harmful peroxides, which generate • Deficiency causes Alkaptonuria (darkening of urine on
free radicals that can cause disruption of cell membranes exposure to air) due to exposure of homogentisate
• Can either be a peroxidase or catalase • Alkaptonuria is a disorder of amino acid catabolism

3.1 Peroxidase

• Reduce peroxides using various electron acceptors

• Prosthetic group is heme [protoheme kay Harpers] (non-
amino acid portion of a protein)
• H2O2 is reduced at the expense of another substance acting
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as an e acceptor
H2O2 + AH2 2H20 + A
Peroxidase

4.1b 3-Hydroxyanthranilate Dioxygenase

• Catalyzes the final enzymatic step in the tryptophan to

quinolinate biosynthetic pathway
• Quinolinate is the precursor to the pyridine ring of the
nicotinamide cofactors

3.1.1 Glutathione Peroxidase

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[Biochemistry] [Biologic Oxidation] Module 2, Lecture 3

syang byproduct nung process. Ang mangyayari ngayon sa

superoxide is either, irereduce nya yung oxidized cytochrome c
(which is important in ATP synthesis kasi isa sya sa mga carrier
don) or ireremove sya ng SOD by converting it pabalik sa oxygen
and hydrogen peroxide. Wag na natin isipin kung bakit masamang
mareduce yung cytochrome c kasi masyado ng complicated basta
lethal sya kasi magkakaron ng build up ng mga molecules na mag-
iinhibit sa function ng cytochrome c.

4.1c L-tryptophan Dioxygenase

• Adds oxygen to tryptophan in tryptophan catabolism

• Tryptophan is a amino acid. Products of tryptophan are
serotonin and it can also lead in the synthesis of melanin
(hormone for regulating our circadian rhythm)
4.2 Monooxygenase
• Also called Mixed-Function oxidases or Hydrolases
• Incorporate only 1 atom of molecular oxygen into the
substrate
• The other oxygen atom is reduced to water
A-H + O2 + ZH2  A-OH + H20 + Z
4.2a Cytochromes P450
SUMMARY:
o Oxidation (loss of electrons) is always accompanied by the
reduction of an electron acceptor
o Oxidoreductase have a variety of functions in metabolism
o Oxidases and dehydrogenases plays a major role in
respiration
o Hydroperoxidases protect the body against damage by free
radicals
o Oxygenases Mediate the hydroxylation of drugs & steroids

• Monooygenases important for the detoxification of drugs and

hydroxylation of steroids (from cholesterol)
• NADH and NADPH donate reducing equivalents
• Electrons are passed to cytochrome P450 involving FAD or
FMN (Class I and Class II)
• Class I consist of an iron sulfur (Fe2S2; an FAD-
containing reductase enzyme) protein and the P450
heme protein
• Class II systems contain cytochrome P450
reductase which passes electron from FADH2 to
FMN
• The cytochromes are oxidized by substrates in a series of
enzymatic reactions collectively known as the hydroxylase
cycle
• Oxygen is reduced by accepting electrons from
cytochrome P450 with one atom incorporating into
H2O and the other into a substrate, usually resulting
into its hydoxylation

• In the endoplasmic reticulum of the liver, cytochromes P450

are found with cytochrome b5 and together have a major role
in drug metabolism and detoxification.
• Cytochrome b5 also has an important role as fatty
acid desaturase

**if you want additional information, pakibasa na lang sa book kasi di

namin alam if yung important for us e important din for you guys 

V. SUPEROXIDE DISMUTASE (SOD)

• Protects aerobic organisms against oxygen toxicity by

converting superoxide to peroxide

**Oxygen can be toxic kasi if ma-generate sya into superoxide

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anion free radical (o2 ). This happens kapag nagkaron ng
additional na electron yung oxygen. Tapos kapag naging
superoxide na sya, magkakaroon na ng free-radical chains
reactions na mag-iincrease ng destructive effects nung superoxide.

Yung superoxide naman nafoform sya kapag yung nareduce na

flavins e ma-reoxidize univalently ng molecular oxygen. So para

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