Riboflavin (B2) Flashcards

1
Q

what are the coenzyme forms of riboflavin (B2)?

A
  • flavin adenine dinucleotide (FAD)
  • flavin mononucleotide (FMN)
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2
Q

what are the functions of riboflavin coenzyme form?

A
  • function as electron transfer reaction (2-step single-electron reactions)
  • energy production in the TCA cycle, electron transport chain and fatty acid oxidation
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3
Q

what is the role of free Riboflavin (B2)?

A

acts as a non-coenzyme form that is absorbed and transported throughout the body

DNA synthesis, antioxidant function (glutathione reductase)

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4
Q

how is riboflavin transported in the tissue cells?

A

transported in its “free form” and converted to FAD/FMN in tissue cells via ATP-dependent reactions. The FAD form becomes free riboflavin in the lumen.

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5
Q

what are the two enzymes that make up riboflavin (free form)?

A

flavin and ribitol

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6
Q

what does FMN stand for?

A

flavin mononucleotide

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7
Q

what does FAD stand for?

A

flavin adenine dinucleotide

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8
Q

what are the sources of riboflavin?

A

milk/dairy, eggs, meats, spinach, legumes, mushrooms, and enriched cereals/breads

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9
Q

what are the functions of riboflavin?

A
  • coenzyme in flavoproteins
  • energy transformation (ETC, oxidative decarboxylation of pyruvate and a-ketoglutarate, TCA cycle, and fatty acid oxidation)
  • reducing enzymes (NADPH, FAD-dependent reductase)
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10
Q

______ is the coenzyme used to combine with oxidized ________ into reduced glutathione (NADP+) + 2 GSH

A

FAD; glutathione

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11
Q

what are the electron donors in glutathione reductase?

A

NADPH

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12
Q

why is glutathione reductase essential?

A

maintains glutathione in reduced state (GSH)

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13
Q

GSH is a key endogenous antioxidant for what (3) things?

A
  1. maintaining SH group in proteins
  2. maintaining heme in Fe2+ state
  3. removal of toxic peroxides
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14
Q

what is thioredoxin reductase (TrxR)?

A

flavoenzyme that reduces thioredoxin

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15
Q

what is thioredoxin (Trx)?

A

proteins acting as antioxidants by facilitating the reduction of other proteins by cysteine thiol-disulfide exchange

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16
Q

what are the purposes of thioredoxins?

A
  • helps ribonucleotide reductase to make DNA
  • electron donor (SH) to ribonucleotide
  • used to regenerate S to SH
17
Q

how is riboflavin digested, absorbed and transported through the body?

A
  • FAD/FMN (coenzyme) in foods are hydrolyzed by phosphatases within the intestinal lumen (converts to free form)
  • carrier-mediated and energy-depended processes absorb the free-form
  • after absorption, free riboflavin is transported in the blood and converted back to the coenzyme form (FAD/FMN) and congregates in the liver, kidney, and heart
  • coenzyme form are bound to apoenzyme and function as prosthetic groups for oxidation-reduction reactions
18
Q

how is the free form of riboflavin converted back to its coenzyme form after absorption?

A

ATP-dependent reactions (in tissue cells)

19
Q

how is riboflavin excreted out the body?

A

primarily in urine with small amount in feces

20
Q

what is the deficiency of riboflavin and what individuals have higher risk?

A
  • ariboflavinosis (acute)
  • individuals with homozygous mutation MTHFR, 677TT
21
Q

large doses of riboflavin are known to treat what?

A

migraine headaches

22
Q

how do we assess nutritional status of B2?

A
  • by measuring the activity of erythrocyte glutathione reductase (if limited activity, an individual has a deficiency)
  • AC 1.1.2 = normal
  • AC >1.4 = deficiency
23
Q

what are the key enzymes riboflavin is involved in?

A
  • succinate dehydrogenase
  • glutathione reductase
  • thioredoxin reductase
24
Q

what are the physiological processes riboflavin is involved in?

A
  • electron transport chain
  • fatty acid oxidation
  • redox reactions