Hemoglobin - Functions and Degradation Flashcards
Two forms O2 is transported by in blood, and their percentages
Dissolved O2 (<2%) HbO2 (>98% total blood O2)
product of the pentose phosphate pathway
NADPH
What if the concentration of NADPH is low?
hemolytic anemia due to too much hemolysis and not enough Hb to carry O2
NADPH produced in RBCs help reduce ____ ______
free radicals
a family of chemicals containing cyclic tetrapyrrole
porphyrins
Number of heme groups in Mb
1
Number of heme groups Hb
4
member of the porphyrins family, hydrophobic, contains ferrous iron
heme
secondary structure of myoglobin
a-helix, 8 regions labelled A-H
tertiary structure of myoglobin
globular
Polar residues are on the surface of myoglobin, why?
so it can be dissolved in aqueous environments
The interior of Mb contains mostly non-polar amino acids, with hydrophobic interactions packing and stabilizing Mb. Name the two exceptions
proximal histidine (His F8) distal histidine (His E7) (proximal and distal relative to the heme)
Where is hemoglobin formed?
Bone Marrow
How many subunits are in hemoglobin?
4
What are the differences between fetal and adult hemoglobin?
Adult - HbA1, a2b2
Fetal - HbF, a2y2
Sickle cell Hb mutation
HbS, a2d2; point mutation causes cells to stick to blood vessels and rupture
Describe the Hb taut structure and its effects
DeoxyHb is constrained by salt bonds among different subunits, thus the binding of the first O2 is difficult
Is binding the 2nd, 3rd, and 4th O2 easier or harder? Why?
Easier, accepting the first O2 weaken the salt bonds and lead to conformational changes (R form, relaxed) that facilitate the binding of oxygen
What color is myoglobin under normal conditions?
dark red
DeoxyHb color
purple-blue, seen during cyanosis