BIOCHEMISTRY

LE DO KHAI 20190626
HOANG TRUNG 20190650
RIBOFLAVIN (VITAMIN
B2)
1.RIBOFLAVIN AND THE FLAVIN COENZYMES
2.METABOLISM OF RIBOFLAVIN
3.METABOLIC FUNCTION OF RIBOFLAVIN
4.RIBOFLAVIN DEFICIENCY
5.RIBOFLAVIN IN FOOD
RIBOFLAV
IN AND
THE
FLAVIN
COENZYM
E
 Riboflavin adenin dinucleotide (FAD)

Ribitol

Isoalloxine ring
 Metabolism of Riboflavin

-Apart from milk and eggs, which contain relatively large

amounts of free riboflavin bound to specific binding proteins

-Most of the vitamin in foods is as flavin coenzymes bound to

enzymes, with about 60% to 90% as FAD

-In foods mostly (80–90%) as FAD and FMN cofactors of

proteins
 Riboflavin binding protein

RfBP of chicken
Homeostasi
s
The Effect of Thyroid Hormones on Riboflavin Metabolism
Catabolism and
Excretion of
Riboflavin
Biosynthesis of Riboflavin
3. METABOLIC FUNCTIONS OF RIBOFLAVIN
Flavin
CoEnzyme
Single and Two-Electron–Transferring Flavoprotein Dehydrogenases
 Nicotinamide
Nucleotide
Disulfide
Oxidoreductases
Glutathione reductase, thioredoxin reductase, and
lipoamide dehydrogenaseare members of a
groupof flavoproteins that contain an active site
disulfide
as well as FAD
 NADPH Oxidase, the Respiratory Burst Oxidase

is the rapid release of reactive

oxygen species (superoxide anion
and hydrogen peroxide) from
different types of cells

Flavin oxidases include d- and l-amino

acid oxidases, and some amine oxidases,
although others are quinoproteins
Molybdenum-Containing Flavoprotein Hydroxylases

- are a ubiquitous class of enzymes which contain

molybdenum in association with a low molecular
weight cofactor

It exists as two interconvertible forms:

1. The xanthine dehydrogenase form catalyzes the
oxidation of xanthine
to hypoxanthine at the expense of NAD+.
2. The xanthine oxidase form cannot utilize NAD+, but
reduces oxygen to
hydrogen peroxide.
 The Role of Riboflavin in the Cryptochromes

One of the mechanisms of DNA repair in bacteria, acting

to reduce cyclobutane dipyrimidines and pyrimidine-
pyrimidone dimers formed by exposure to UV light, is the
blue light-activated photolyase
The primary light-trapping pigment is 5,10-methylene
tetrahydrofolate
then transfers the excitation energy of the trapped photon to
FADH, which reduces the
substrate
4.Riboflavin Deficiency

Causes:
+) Inadequate intake
+) Impaired absorption due to intestinal diseases
+) Chronic alcoholics are susceptible to B, deficiency
Clinical features:
+) Cheilosis (fissures at the corners of mouth)
+) Glossitis (tongue smooth and purplish)
+) Corneal vasculalarization: includes dryness, burning &
itching and lacrimination
+) Measurement of glutathione reductase in erythrocytes is a
reliable diagnostic test to assess riboflavin deficiency
+) Reference interval
+) Serum or plasma level is 4 to 24 ug/ dl
 5.Riboflavin in food
Life Stage Recommended Amount
Birth to 6 months 0.3 mg

Infants 7–12 months 0.4 mg

Children 1–3 years 0.5 mg

Children 4–8 years 0.6 mg

Children 9–13 years 0.9 mg

Teen boys 14–18 years 1.3 mg

Teen girls 14–18 years 1.0 mg

Men 1.3 mg

Women 1.1 mg

Pregnant teens and women 1.4 mg

Breastfeeding teens and women 1.6 mg

Reference

Nutritional Biochemistry of the Vitamin (second editio), DAVID A.BENDER

https://www.webmd.com/diet/foods-high-in-riboflavin#1
THANK YOU !