Vitamins As Coenzymes & Cofactors

Most vitamins act as coenzymes or are required for the synthesis of coenzymes
are water-soluble ones. In all cases except vitamin C, the vitamin must be
modified before it can serve its function.
Vitamins
Coenzymes
Thiamine (B1)
Thiamine pyrophosphate
Flavin adenin dinucleotide
(FAD)
Flavin adenine
mononucleotide (FMN)
Nicotiamide adenine
dinucleotide (NAD+)
Nicotinamide adenine
dinucleotide phosphate
(NADP)
Riboflavin (B2)
Niacin
(Nicotiamide/Nico
tinic acid) (B3)
Pantothenic acid
(B5)
Coenzyme A (CoA)
Pyridoxine (B6)
Pyridoxal phosphate
Biotin (B7)
Biotin lysin complexes

(biocytin)
Folic acid (B9)
Tetrahydrofolate
Cobalamin (B12)
5-deoxyadenosyl cobalamin
Methylcobalamin
Ascorbic acid (C)
None
Vitamin K
Menaquinone
Typical reaction
type
Decarboxylation
Oxidation Reduction
Oxidation Reduction
involving the
hydride ion (H)
Acyl-group transfer
Variety of reactions
including the transfer
of amino groups
ATP-dependent
carboxylation and
carboxyl-group
transfer
Transfer of onecarbon units such as
the formyl group
Transfer of methyl
groups;
intramolecular
rearrangement
Transfer of electrons
Transfer of carbonyl
groups and electrons
Three classes of vitamin-derived coenzymes used to carry electrons: the

nicotinamide coenzymes, the flavin coenzymes, and ascorbic acid.
The others act as carrier of functional groups such as amino, carbonyl, acyl,
methyl or participate in typical reactions such as decarboxylation
Vitamin B3:
Niacin is required for the synthesis of two coenzyme molecules: NAD and NADP.
NAD and NADP act as soluble electron carriers between proteins. In effect,
these compounds are substrates for enzymes involved in oxidation and

reduction reactions. NAD is primarily involved in catabolic reactions by
accepting electrons during the breakdown of molecules for energy. In contrast,
NADPH (the reduced form of NADP) is primarily involved in biosynthetic
reactions by donating electrons required for synthesizing new molecules. In
most cells, NAD levels are much higher than NADH levels, while NADPH levels
are much higher than those of NADP.
The two possible electronic states for the nicotinamide cofactors are shown
below:
The oxidized forms of both nicotinamide coenzymes can only accept electrons
in pairs. The reduced forms of the coenzymes can only donate pairs of
electrons.
An example of the role of NAD in redox chemistry is provided by the
oxidoreductase enzyme liver alcohol dehydrogenase. Alcohol dehydrogenase
can catalyze the oxidation of several different alcohols. In each case it uses
NAD as the electron acceptor. The active site is thus moderately non-specific
for the alcohol, although it is quite specific for NAD compared to NADP.
The mechanism of alcohol dehydrogenase thus includes transition state
stabilization (the stabilization of the negative charge on the substrate oxygen
in particular), as well as acid-base catalysis. It also illustrates the marked
changes in pKa values that can occur in specific environments.
Vitamin C
as a Cofactor in Collagen Formation Vitamin C helps to form the fibrous

structural protein of connective tissues known as collagen. During the synthesis
of collagen, each time a proline or lysine is added to the protein chain, the
enzyme prolyl hydroxylase will add an OH group to the amino acid, making it
hydroxyproline or hydroxylysine, respectively. The conversion of proline to
hydroxyproline requires both vitamin C and iron. Iron works as a cofactor in the
reaction, and vitamin C protects iron from oxidation, thereby allowing iron to
perform its duty.
as a Cofactor in Other reactions Vitamin C also serves as a cofactor in the
synthesis of several other compounds. As in collagen formation, vitamin C helps in
the hydroxylation of carnitine, a compound that transports fatty acids, especially
long-chain fatty acids, across the inner membrane of mitochondria in cells. It also
participates in the conversions of the amino acids tryptophan and tyrosine to the
neurotransmitters serotonin and norepinephrine, respectively. Vitamin C also
assists in the making of hormones, including thyroxine, which regulates the
metabolic rate; when metabolism speeds up in times of extreme physical stress,
the bodys use of vitamin C increases.
Vitamin K
Of all fat-soluble vitamins, vitamin K is the only one that acts as a classical
coenzyme. Vitamin K is required as a enzyme cofactor in the synthesis of carboxyglutamic acid. The reduced form of vitamin K acts as coenzyme for the
carboxylase that turn a glutamate amino acid residue in a protein into a gammacarboxyglutamate (Gla) residue. The domain containing this post-translational
modification is critical for the interaction of the vitamin K-dependent clotting
factors with negatively charged phospholipid membranes calcium bridging.
Vitamin B2
Riboflavin is the precursor to the flavin coenzymes FMN and FAD. Flavins are
yellow in color and are light sensitive (flavins in food left out in the sun degrade
fairly rapidly). FMN and FAD are non-covalently attached to their enzymes, but
generally do not dissociate. These compounds therefore nearly always function
as prosthetic groups, and act as storage locations for electrons within proteins.
The isoalloxazine ring can accept or transfer electrons one at a time, although
they can carry up to two electrons. This ability to accept either one or two
electrons is often of critical importance for biological reactions. The structures
below show the different electronic states observed for both flavin coenzymes.
The partially reduced form contains a radical (note that the carbon with the
has only three actual bonds). This form of the compound (technically known as
the semiquinone form of the isoalloxazine ring) is actually fairly stable. It is the
relative stability of this state which allows flavin-containing enzymes the flexibility
of transferring electrons either one or two at a time. The flavin and nicotinamide
coenzymes are critically important electron carriers for a wide variety of biological
processes. Both types of coenzymes are used by a number of enzymes. The
nicotinamide coenzymes are used for carrying pairs of electrons between
proteins, while the flavins primarily function as temporary storage for electrons
within proteins.
Folic acid:
Folate must be converted to the active form, tetrahydrofolate, by dihydrofolate
reductase.
Tetrahydrofolate acts as a single carbon carrier. The carbon can be present in

most of the possible oxidation states for carbon with the exception of carbonate.
The carbon unit is attached to the tetrahydrofolate molecule at the N5-position,
N10- position, or using an arrangement that bridges both positions.
Tetrahydrofolate is required for a number of biosynthetic enzymes. During
thymidine synthesis (in the conversion of dUMP to dTMP catalyzed by thymidylate
synthase), tetrahydrofolate is converted to dihydrofolate; the dihydrofolate must
be reduced to tetrahydrofolate to restore the active cofactor. Because thymidine
is required to synthesize DNA, and because dividing cells must synthesize DNA,
inhibition of dihydrofolate reductase (e.g., by methotrexate) prevents cell division.
Because of its importance to growing cells, folate is required to prevent some
types of birth defects. In adults, folate deficiency causes megaloblastic anemia.
Folic acid is the source of the methyl group donated by methylcobalamin in the
methionine synthase reaction, and therefore folic acid deficiency shares some
symptoms with vitamin B12 deficiency
Vitamin K
Of all fat-soluble vitamins, vitamin K is the only one that acts as a classical
coenzyme. Vitamin K is required as a enzyme cofactor in the synthesis of carboxyglutamic acid. -Carboxyglutamic acid is formed as a post-translational
modification required for some proteins. This unusual amino acid residue is
important for the function of a number of proteins, the most notable being some
of the clotting factors. The synthesis of -carboxyglutamate from glutamate
residues is a cycle (see figure below). The reduced form of vitamin K acts as
coenzyme for the carboxylase that produces the modified glutamate side-chain
(note that this carboxylase does not require biotin)

Vitamins As Coenzymes & Cofactors

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Most vitamins act as coenzymes or are required for the synthesis of coenzymes

Biotin lysin complexes

Folic acid (B9)

Ascorbic acid (C)

Three classes of vitamin-derived coenzymes used to carry electrons: the

these compounds are substrates for enzymes involved in oxidation and

as a Cofactor in Collagen Formation Vitamin C helps to form the fibrous

Tetrahydrofolate acts as a single carbon carrier. The carbon can be present in

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