Hemoglobin Flashcards
Where is myoglobin found
found in muscle for oxygen storage
Single ferous _____- containng heme prosthetic group in protective hydrophobic pocket binds oxygen
Fe++
If oxidized to ferric (Fe+++)
it binds H20
what is myoglobins conformation stabilized by
hydrophobic interactions
Posterior 93 His (proximal) binds:
Fe++
Distal His provides ___ ____ for unfavorable interactions
steric hindrance (CO)
What is a heme
4 pyrrole ring structures linked by methene bridges= porphyrin ring
When you add specific side groups to a heme its called:
protophorphyrin IX
A heme is not considered a heme until you add
Fe++ = heme
Where is heme found
oxygen transporter, and storage proteins and cytochromes
Myoglobin has ____ alpha helical conformation
75% (8 regions)
Myoglobins saturation curve is ____ and is indicative of its function.
hyperbolic; store oxygen until its critically needed
Hematopoietic stem cell directed to erythroid lineage by the hormone
erythropoietin
Hemoglobin relies on ___ and ___ for energy
glucose and glycolysis
Small ___shape allows passage through capillaries
concave
Hemoglobin is found in ____ for ____ transport.
RBC’s; oxygen
Hemoglobin is a tetramer that has 2 ___chains and 2 ___chains. Thus Hb has a quaternary structure and exhibits _____
alpha; beta; cooperativity
What are the similarities between Mb and Hb
- Each has 8 alpha helical regions connected by beta turns.
- Heme prosthetic group
- Distal and proximal histidines
Hemoglobin is designed to deliver oxygen :
all the time; therefore it has a sigmoidal curve
Myoglobin delivers oxygen only when partial pressure of oxygen is:
low; only delivers when need; therefore the curve is hyperbolic
What is the embryonic Hb like
zeta and epsilon chains
What is fetal Hb like
Adult alpha and fetal Beta like (gamma) are expressed during the 2nd and 3rd trimesters.