WGU BIOCHEMISTRY OA EVALUATION EXAM 2025/2026
QUESTIONS WITH ANSWERS RATED A+
✔✔Fxn of myoglobin
Where is it stored
How does it bind to o2 - ✔✔Oxygen storage
stores in the muscle cell
binds to o2@ low o2 levels tightly (its reaches saturation quickly)
✔✔Hemoglobin fxn - ✔✔oxygen transport
✔✔How much subunits to o2 molecules for hemoglobin? - ✔✔4 subunits =4 o2
molecules
✔✔What two states does hemoglobin exist in and why? - ✔✔1.R-state (relaxed) oxygen
in bound to it- it attaches to the heme complex and causes it be planar
2. T-state (stressed state) oxygen is not bound to it; the FE atom pulls on it and causes
it to slightly bend altering the light absorption of the porphyrion ring giving venous blood
a deep purple color
✔✔How does hemoglobin differ from myoglobin in concentration? - ✔✔Require a much
higher o2 concentration to bind
binds tightly to o2 in the lungs
✔✔What molecules influence the affinity of hemoglobin for o2? What state does it
cause it to be in (T or R)? which way would it cause the curve to shift? - ✔✔CO-
stablizes the "R" state-shifts left
2-3 BPG stabllizes the "T" state-shifts right
H+stables the "T" state-shifts right
------These contribute to the Bohr effect and the impact Ph has on O2 binding
✔✔Myoglobin graph is - ✔✔hyperbolic shape
---it increase rapidly
--direct relationship with Po2- and the Po2 increases the binding of o2 to myoglobin
increases to (90% saturated at 20 torr.)
✔✔How would the o2 carrying capacity be meausred? - ✔✔Hemotocrit and % blood
volume
Normal ranges: 40% women, 45% men
✔✔Graph of hemoglobin - ✔✔Sigmodial shape
✔✔Why does hemoglobin has a low o2 affinity - ✔✔because of it quaternary structure
, ✔✔T state favor which environment and what is the effects - ✔✔Favors low PH (highly
acidic environment; H+ concentrations)
-Low affinity for o2 in this state
-induces o2 release
-this o2 is picked up by cells in need of o2
-Hb releases 10% more o2 at Ph of 7.2 compared to 7.4
--MORE CO2 means MORE acidic
✔✔R state favors which environment and what is the effects - ✔✔Favors high Ph (More
basic; less H+ concentrations)
-High affinity for o2 in this state
-stimulates the binding of o2; o2 binds more tightly as PH increases
---As acidiosis occurs less o2 is being circulated, this causes the o2 on Hb to remain
bound (it wont release) This decreases o2 affinity for o2-thus CO increases
✔✔Myoglobin has which helices? - ✔✔Alpha helices
✔✔Hemoglobin has which helices? - ✔✔Alpha and beta helices
✔✔What makes fetal Hb different? - ✔✔It doesn't bind to 2,3BPG. B/c of this the fetal
Hb has a higher affinity for o2.
It binds tighter to o2 than the mother
✔✔What role does 2,3 BPG has on o2? - ✔✔It stimulates o2 release in the tissues
--it binds to the deoxy. form of Hb and stablizes the T state-->this causes a decrease in
the Hb affinity for o2 which allows more o2 in the tissues
---decrease o2 affinity
---allows o2 to be released.
✔✔Sickle cell is mutation of which subunit for which protein? - ✔✔Beta subunit of Hb
✔✔Metabolic pathway - ✔✔series of biochemical rxn needed to go from raw material to
final product
✔✔catabolic pathway - ✔✔break large molecules down
include "lytic"
releases energy trapped in chemical bonds
✔✔Which bonds contain the highest amt of energy in the form of ATP? - ✔✔bonds
between phosphates
✔✔Anabolic Pathway - ✔✔Pathways THAT USE energy from ATP to build compounds
-include the "genesis"
QUESTIONS WITH ANSWERS RATED A+
✔✔Fxn of myoglobin
Where is it stored
How does it bind to o2 - ✔✔Oxygen storage
stores in the muscle cell
binds to o2@ low o2 levels tightly (its reaches saturation quickly)
✔✔Hemoglobin fxn - ✔✔oxygen transport
✔✔How much subunits to o2 molecules for hemoglobin? - ✔✔4 subunits =4 o2
molecules
✔✔What two states does hemoglobin exist in and why? - ✔✔1.R-state (relaxed) oxygen
in bound to it- it attaches to the heme complex and causes it be planar
2. T-state (stressed state) oxygen is not bound to it; the FE atom pulls on it and causes
it to slightly bend altering the light absorption of the porphyrion ring giving venous blood
a deep purple color
✔✔How does hemoglobin differ from myoglobin in concentration? - ✔✔Require a much
higher o2 concentration to bind
binds tightly to o2 in the lungs
✔✔What molecules influence the affinity of hemoglobin for o2? What state does it
cause it to be in (T or R)? which way would it cause the curve to shift? - ✔✔CO-
stablizes the "R" state-shifts left
2-3 BPG stabllizes the "T" state-shifts right
H+stables the "T" state-shifts right
------These contribute to the Bohr effect and the impact Ph has on O2 binding
✔✔Myoglobin graph is - ✔✔hyperbolic shape
---it increase rapidly
--direct relationship with Po2- and the Po2 increases the binding of o2 to myoglobin
increases to (90% saturated at 20 torr.)
✔✔How would the o2 carrying capacity be meausred? - ✔✔Hemotocrit and % blood
volume
Normal ranges: 40% women, 45% men
✔✔Graph of hemoglobin - ✔✔Sigmodial shape
✔✔Why does hemoglobin has a low o2 affinity - ✔✔because of it quaternary structure
, ✔✔T state favor which environment and what is the effects - ✔✔Favors low PH (highly
acidic environment; H+ concentrations)
-Low affinity for o2 in this state
-induces o2 release
-this o2 is picked up by cells in need of o2
-Hb releases 10% more o2 at Ph of 7.2 compared to 7.4
--MORE CO2 means MORE acidic
✔✔R state favors which environment and what is the effects - ✔✔Favors high Ph (More
basic; less H+ concentrations)
-High affinity for o2 in this state
-stimulates the binding of o2; o2 binds more tightly as PH increases
---As acidiosis occurs less o2 is being circulated, this causes the o2 on Hb to remain
bound (it wont release) This decreases o2 affinity for o2-thus CO increases
✔✔Myoglobin has which helices? - ✔✔Alpha helices
✔✔Hemoglobin has which helices? - ✔✔Alpha and beta helices
✔✔What makes fetal Hb different? - ✔✔It doesn't bind to 2,3BPG. B/c of this the fetal
Hb has a higher affinity for o2.
It binds tighter to o2 than the mother
✔✔What role does 2,3 BPG has on o2? - ✔✔It stimulates o2 release in the tissues
--it binds to the deoxy. form of Hb and stablizes the T state-->this causes a decrease in
the Hb affinity for o2 which allows more o2 in the tissues
---decrease o2 affinity
---allows o2 to be released.
✔✔Sickle cell is mutation of which subunit for which protein? - ✔✔Beta subunit of Hb
✔✔Metabolic pathway - ✔✔series of biochemical rxn needed to go from raw material to
final product
✔✔catabolic pathway - ✔✔break large molecules down
include "lytic"
releases energy trapped in chemical bonds
✔✔Which bonds contain the highest amt of energy in the form of ATP? - ✔✔bonds
between phosphates
✔✔Anabolic Pathway - ✔✔Pathways THAT USE energy from ATP to build compounds
-include the "genesis"
