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WGU BIOCHEM Module 3

Myoglobin and Hemoglobin

______________ is a protein consisting of a single subunit that contains a heme group with an iron atom bound. the iron atom binds one molecule of oxygen myoglobin
_______________ is a tetramer protein containing two alpha and two beta global subunits. hemoglobin
hemoglobin has __________ structure, while myoglobin has only ______________ structure because it has only one subunit quaternary, tertiary
each subunit contains a heme molecule and an iron atom, allowing each hemoglobin protein to bind _____ molecules of oxygen 4
hemoglobin structure is very sensitive to ____________ binding oxygen
oxygenated form relaxed or "R" state
deoxygenated form tense or "T" state
hemoglobin's function oxygen transport
# of subunits in myoglobin 1
# of subunits in hemoglobin 4
addition of ____________ alters the shape of the iron-heme complex, and therefore its absorption of light as indicated by its color change from dark purple to brilliant scarlet porphyrin
myoglobin binds oxygen reversibly in response to ____________________ oxygen concentration
myoglobin function bind and store oxygen for muscles to use when blood oxygen is low
bohr effect: at high ph hemoglobin has a _____ affinity for oxygen, while at low ph it has a _____ affinity for oxygen and tends to release it high; low
2,3-BPG binds to _____________ hemoglobin and stabilizes the _____ state of the protein deoxygenated; T
carbonic anhydrase is an enzyme which catalyzes the conversion of carbon dioxide to _____________________ ions bicarbonate
hemoglobin acts as a buffer and controls the ph of the blood by binding to __________ H+ ions
in locations where the ph is low, hemoglobin will begin the _______ state, allowing it to ________ oxygen more efficiently T; release
carbon ___________ decreases hemoglobin's affinity for oxygen, while carbon _______________ increases it dioxide; monoxide
hemoglobin binds to carbon monoxide with a __________ affinity than oxygen and stabilizes the _______ state higher; R
when hemoglobin changes from T to R, it has __________ affinity for oxygen high
when hemoglobin changes from R to T, it has ________ affinity for oxygen low
______________ refers to hemoglobin structural changes that increase its affinity for oxygen cooperativity
when oxygen concentration is high, heme shape is ______________. when oxygen concentration is low, heme shape is _______________ planar; bent
relative to the lungs, the ph in the peripheral tissues is ________ because ______________ lower, the CO2 generated by metabolism is converted to bicarbonate, which releases protons (H+)
when the H+ ion concentration increases, the ph of the solution ____________ decreases
myoglobin has a _______ affinity for oxygen compared to hemoglobin higher
________________ has a signmoidal curve, where as ______________ has a hyperbolic curve hemoglobin; myoglobin
which atom helps oxygen bind to hemoglobin iron
the T state is favored by ___________pH and induces the ___________ of oxygen low; release
relative to the peripheral tissues, the ph in the lungs is ___________ because __________________ higher; the protons (H+) that were combined with hemoglobin quickly bind to bicarbonate to form CO2, and then is exhaled
carbon monoxide binds to hemoglobin ______ times better than oxygen 200
when the blood ph is low, the heme is in ___________ shape when the blood ph is high, the heme is in ____________ shape bent; planar
Created by: kinseycharles
 

 



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