Porphyrins and Hemoglobin Structure

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Questions and Answers

What is a porphin?

  • A type of hereditary disease
  • A cyclic compound formed by the linkage of 4 pyrrole rings (correct)
  • A protein that contains heme as a prosthetic group
  • A complex of one porphyrin and ferrous iron

What is the function of the heme group in hemoglobin and myoglobin?

  • To interact with oxygen and form damage oxygen radicles
  • To reversibly bind oxygen (correct)
  • To catalyze the breakdown of hydrogen peroxide
  • To serve as an electron carrier

What is the result of a deficiency of one of the enzymes needed for heme synthesis?

  • Increased production and excretion of porphyrins and/or their precursors (correct)
  • Decreased production and excretion of porphyrins and/or their precursors
  • Only increased production of porphyrins
  • No effect on porphyrins and/or their precursors

What type of porphyria is caused by lead poisoning?

<p>Any type of porphyria (B)</p> Signup and view all the answers

What is the function of the heme group in catalase?

<p>To catalyze the breakdown of hydrogen peroxide (B)</p> Signup and view all the answers

What is the result of anemia in patients with porphyria?

<p>Decreased production of heme (B)</p> Signup and view all the answers

What is the result of photosensitivity in patients with porphyria?

<p>Formation of damage oxygen radicles (D)</p> Signup and view all the answers

What is the inheritance pattern of congenital erythropoietic porphyria?

<p>Autosomal recessive (D)</p> Signup and view all the answers

What is the primary function of myoglobin in muscle cells?

<p>To act as a reservoir and carrier for oxygen (B)</p> Signup and view all the answers

What is the structure of the myoglobin molecule?

<p>A compact molecule with 80% α-helix structure (D)</p> Signup and view all the answers

How many oxygen molecules can myoglobin bind?

<p>One (A)</p> Signup and view all the answers

What is the partial pressure of oxygen needed to achieve half-saturation of the binding sites on myoglobin?

<p>1 mm Hg (A)</p> Signup and view all the answers

What happens to the oxygen dissociation curve when the pH is raised or the concentration of CO2 in the lungs is lowered?

<p>It shifts to the left (A)</p> Signup and view all the answers

What is the Bohr effect?

<p>The decrease in oxygen binding capacity of hemoglobin at low pH (B)</p> Signup and view all the answers

What happens to the oxygen dissociation curve in the Bohr effect?

<p>It shifts to the right (D)</p> Signup and view all the answers

What is the effect of 2,3-bisphosphoglycerate (2,3 BPG) on the oxygen affinity of hemoglobin?

<p>It decreases the oxygen affinity (A)</p> Signup and view all the answers

What is the purpose of 2,3-BPG in the RBCs?

<p>To release oxygen efficiently in the tissues (B)</p> Signup and view all the answers

What is the primary difference in oxygen binding between myoglobin and hemoglobin?

<p>Myoglobin has a higher oxygen affinity than hemoglobin (C)</p> Signup and view all the answers

What happens to the oxygen affinity of hemoglobin in the absence of 2,3-BPG?

<p>It increases (C)</p> Signup and view all the answers

What is the function of the heme group in myoglobin?

<p>To bind oxygen (B)</p> Signup and view all the answers

What is the function of Hb A2?

<p>It is synthesized in the adult at low levels compared to Hb A (D)</p> Signup and view all the answers

What can happen to Hb A?

<p>It can become modified by the covalent addition of a hexose (D)</p> Signup and view all the answers

What occurs due to an imbalance in the synthesis of globin chains in thalassemias?

<p>A defect in either α or β-globin chain synthesis (C)</p> Signup and view all the answers

What leads to the formation of α2β2 (Hb A) in normal conditions?

<p>Coordination in the synthesis of α and β-globin chains (A)</p> Signup and view all the answers

Which enzyme catalyzes the first step in the degradation of heme?

<p>Heme oxygenase (D)</p> Signup and view all the answers

What pigment is produced as a result of the first step in the degradation of heme?

<p>Biliverdin (C)</p> Signup and view all the answers

How is bilirubin transported to the liver?

<p>Bound to albumin (D)</p> Signup and view all the answers

What increases the solubility of bilirubin in the hepatocyte?

<p>Addition of glucuronic acid (B)</p> Signup and view all the answers

What is formed when bilirubin diglucuronide is hydrolyzed and reduced by bacteria in the gut?

<p>Urobilinogen (C)</p> Signup and view all the answers

What is the primary location where red blood cells are degraded after approximately 120 days in circulation?

<p>Reticuloendothelial system (D)</p> Signup and view all the answers

What pigment gives feces its characteristic brown color?

<p>Stercobilin (D)</p> Signup and view all the answers

What is the main cause of hemolytic jaundice?

<p>Massive lysis of red blood cells (B)</p> Signup and view all the answers

What is the fate of reabsorbed urobilinogen in the portal blood?

<p>Participates in the enterohepatic urobilinogen cycle (B)</p> Signup and view all the answers

Which type of jaundice involves an obstruction of the bile duct?

<p>Obstructive jaundice (C)</p> Signup and view all the answers

What causes the urine to turn dark in hepatocellular jaundice?

<p>Increase in urobilinogen (C)</p> Signup and view all the answers

Why do newborns often develop jaundice?

<p>Immature liver function (B)</p> Signup and view all the answers

What enzyme's activity is low at birth, contributing to jaundice in newborns?

<p>Hepatic bilirubin glucuronyltransferase (B)</p> Signup and view all the answers

What is the end product of heme catabolism?

<p>Bilirubin (B)</p> Signup and view all the answers

Flashcards

What is a porphin?

A cyclic compound formed by the linkage of 4 pyrrole rings

Heme group function

To reversibly bind oxygen

Enzyme deficiency result

Increased production and excretion of porphyrins and/or their precursors

Porphyria cause

Any type of porphyria

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Catalase function

To catalyze the breakdown of hydrogen peroxide

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Anemia result

Decreased production of heme

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Photosensitivity result

Formation of damage oxygen radicles

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Inheritance pattern

Autosomal recessive

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Myoglobin function

To act as a reservoir and carrier for oxygen

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Myoglobin structure

A compact molecule with 80% α-helix structure

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Oxygen molecules bound

One

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Partial pressure needed

1 mm Hg

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Oxygen dissociation curve shift

It shifts to the left

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What is the Bohr effect?

The decrease in oxygen binding capacity of hemoglobin at low pH

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Curve shift in Bohr effect

It shifts to the right

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BPG effect

It decreases the oxygen affinity

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Purpose of 2,3-BPG

To release oxygen efficiently in the tissues

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Oxygen binding difference

Myoglobin has a higher oxygen affinity than hemoglobin

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Oxygen affinity change

It increases

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Heme group function

To bind oxygen

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Function of Hb A2

It is synthesized in the adult at low levels compared to Hb A

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Hb A changes

It can become modified by the covalent addition of a hexose

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Imbalance result

A defect in either α or β-globin chain synthesis

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Formation of Hb A

Coordination in the synthesis of α and β-globin chains

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First enzyme

Heme oxygenase

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Pigment produced

Biliverdin

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Bilirubin transport

Bound to albumin

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Solubility increase

Addition of glucuronic acid

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Bilirubin diglucuronide result

Urobilinogen

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Primary location

Reticuloendothelial system

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