BIOLOGICAL OXIDATION

Redox potential and classification of oxidoreductases

Lecture 1
Department of Biochemistry
NKP Salve Institute of Medical Sciences, Nagpur
 At the end of the lecture the student should be able to

no Learning objectives Domain Competency

level
1. Define biological oxidation. Cognitive Must know

2. Classify enzymes in biological Cognitive Must know

oxidation
 BIOLOGICAL OXIDATION

INTERMEDIARY METABOLISM
Anabolism Catabolism
Why energy?

Chemical Potential? Free Energy?

FREE ENERGY---------exergonic and endergonic

anabolism and catabolism
+ G&- G
 PHOSPHAGENS
PHOSPHAGENS – high energy phosphate
compounds

LIPMAN`S SIGN ():

ATP -7.3, cAMP -12.0,

creatine phosphate -10.3,
1,3 diphosphoglycerate -11.8
Acetyl phosphate -12.8,
phosphoenol pyruvate -14.8
 OXIDATION – REDUCTION
• Involves the transfer of electrons:

oxidation - addition of O or removal of

electrons, H
reduction – removal of O or addition of
electrons, H

Oxidation is always Hence OR redefined as

accompanied by Transfer of
Simultaneous reduction Reducing Equivalents
 Fe ++
Catabolism/Exergonic/Oxidation
Ferrous Fe +++Ferric
Reductant
e donor

e-
Cu++
Cu+ Cuppric
Cupprous Anabolism/Endergonic/Reduction Oxidant
e acceptor
O-R redefined as
Can we redefine TRANSFER OF
Oxi-Red reactions REDUCING
EQUIVALENTS
 Oxidation Reduction Potential
Redox Potential

Tendency of a substance to donate or accept

Reducing Equivalents

Free Energy Change = Redox Potential

At pH 7
Eo of H electrode
-0.42voltes
 Redox Potentials of Mammalian Redox Systems

More negative
Redox potential
Oxygen/water +0.82
Means greater
Cyto a +0.29 Tendency to
Cyto c +0.22 Lose electrons
Cyto b-2 +0.12 And vice versa
Ubiquonone cyto Q +0.10
Electrons flow
Cyto b +0.08 from a redox pair
FMN/FAD -0.12 That is
NAD/NADH -0.32 More Electronegative
H+/H2 -0.42 to
More Electropositive
 COUPLING OF EXERGONIC AND ENDERGONIC REACTIONS

One way :
Forming ATP in
Exergonic and using
Same in Endergonic

Other way:
AH2 carrier interm`te BH2
Using
Common
intermediate
Which actually
A carrier Inter H2 B
Takes part
In the reaction
 O-R REACTIONS IN BIOLOGICAL SYSTEMS
1] Removal of red. Eq from
Metabolite to O2 directly

Single large potential jump

Recovery of free energy not total
Loss of free energy
2]

Metabolite a b c d O2

Removal in series Small potential jump

Of steps with Energy liberate din small fractions
Recovery of free energy efficient
Number of Enzymes
Involves enzymes and coenzymes
(Class ? IUB?)
 OXIDOREDUCTASES class 1 of IUB
enzymes involved in oxidation reduction

OXIDASES
AEROBIC DEHYDROGENASES
ANAEROBIC DEHYDROGENASES
HYDROPEROXIDASES
OXYGENASES
 OXIDASES

•Catalyses the removal of H from substance

•Uses only O as H acceptor
•H20 almost always the end product
•Exception : MAO, Uricase: H2O2
•Used in the last step in ETC
•Ex: Cytochrome oxidase, ascorbic oxidase,
phenolase
 AEROBIC DEHYDROGENASE

•Catalyses the removal of H from substance

•Uses either O or artificial substance like methylene blue as
H acceptor
• H2O2the end product
•Are metallo FLAVOPROTEINS: FMN, FAD(vit:- riboflavin)
•Eg: FAD: LAA DH, Aldehyde DH, xanthine Dh, Glucose
oxidase FMN: D AA DH
•FAD+2H FADH2
•FMN+2H FMNH2
 Catalyses removal of H
ANEROBIC DEHYDROGENASE From substrates but
Unable to use O as
acceptor
Perform 2 main functions:
1. Transfer hydrogen from one substrate to another
in a coupled O/R reaction
2. As components of Electron transport chain

use coenzymes
nicotinamides &
riboflavin
as
hydrogen
carriers
 CLASSIFICATION OF ANAEROBIC DH
1. Anaerobic DH dependent on nicotinamide coenzyme
NAD / NADP as coenzyme from vitamin niacin
Eg:
NAD requiring DH – glycolysis, beta oxidation of Fatty acids, TCA, ETC
NADP requiring DH- HMPS, Fat and steroid synthesis

NAD + Reducing subs Oxidised subs+NADH + H+

NADP + Reducing subs Oxidised subs+NADPH + H+

NAD Linked NADP Linked

Malate DH Glu 6P DH
Lactate DH 6P gluconate DH
Gly 3 P DH Isocitrate
Pyruvate DH DH(extramito)
α KG DH
Isocitrate DH(mito)
2. Anaerobic DH dependent on riboflavin coenzyme

•Similar to aerobic DH but cannot give reducing equivalent to

molecular oxygen nor yield H2O2 as product.
•More tightly bound than NAD.
•In ETC
•Eg: Succinate DH, Acyl CoA DH, Glycerol P DH, Pyruvate DH, α KG DH

3. Cytochromes
•Except cyto oxidase all are anaerobic DH
•In ETC
•Iron containing HEMOPROTEIN in which Fe OSCILLATES between
Fe +++ and Fe++
•Eg: cyto b, cyto c1, cyto c
•Also found in endoplasmic reticulum of plant, bacteria and yeast –
cyto P – 450, cyto b5
 Hydroperoxidases
• Found in milk, leucocytes, platelets.
• Utilize H2O2 from aerobic DH reactions
• CATALASE AND PEROXIDASE
• Peroxidases reduce H2O2 at the expense of several other substances
(ascorbic acid, glutathione, iodides, vit E, cyto C)

H2O2 + AH2  2H2O + A

Eg: Glutathione peroxidase, iodine peroxidase, cyto C peroxidase

• Catalase uses H2O2 as electron acceptor & electron donor

2H2O2  2H2O
Peroxisomes are rich in oxidases and catalases
 Oxygenases
• Catalyse the incorporation of O2 into subtrates
• Reactions other than energy(synthetic and degradation)
Consists of two sets of enzymes
 Dioxygenases :
incorporate both atoms
of oxygen into the substrate ;
A + O2  AO2

Eg: Homogentisate dioxygenase,

Tryptophan dioxygenase,
Carotene dioxygenase
 Monooxygenases : (mixed function oxidase, hydrolase)
incorporates one atom of oxygen into substrate
& other is reduced to water
A – H + O2 + ZH2  A – OH + H2O + Z
Found in microsome of liver with cyto P 450 and cyto b5
Need coenzymes :
tetrahydrobiopterin, L ascorbic acid, cyto P450 and NADPH
Eg: Phenylalanine hydroxylase,
kynurenine 3 hydroxylase,
steroid synthesis,
metabolism of drugs
 Summary
• Oxidation reduction
• Redox potential
• Classification of enzymes involved in
oxidation and reduction
 Bibliography
1.Harper’s Illustrated Biochemistry, 8th Edi.
Murray & Bender
2. Text Book of Biochemistry,6th edi.
Vasudevan & Sreekumari S
 Commonly asked questions in university
exams
• Define oxidation and reduction.(4m)
• Classify enzymes of oxidation and reduction.
(8m)
Thank you