CHEMISTRY OF RESPIRATION Flashcards
heme proteins that maintain a supply of oxygen essential for oxidative metabolism
myoglobin
hemoglobin
myoglobin is rich in ____ helices
alpha helices
5th coordination position of iron is linked to a ring nitrogen
proximal histidine / His F8
lies on the side of the heme ring opposite to His F8
Distal Histidine/ His E7
___________ provides a hindered environment for heme iron
apomyoglobin
the distal E7 histidine hinders bonding of carbon dioxide at the preferred _______ angle to the plane of the heme ring
90 degree
in oxygenation of myoglobin accompanied motion of the iron, _______ and of residues linked to _______
His F8
a tetrameric protein of erythrocytes
transports oxygen to tissues and returns carbon dioxide and protons to the lungs
hemoglobin
hemoglobins bind ____ molecules of oxygen per tetramer one per heme
4
hemoglobin has a ________curve
sigmoid
myoglobin has a __________ curve
hyperbolic curve
iron is not aligned with the heme plane
in the 6th coordination position of iron, it is not bound to oxygen yet
T state
iron is aligned with the heme plane
oxygen is bound to iron already
iron moves into plane of heme and pulls proximal histidine along with it
R state oxyhemoglobin
a phenomenon permitting hemoglobin to maximize both the quantity of oxygen loaded at the PO2 of the lungs and the quantity of O2 released at the PO2 of the peripheral tissues
cooperative tissues
__________ is an organophosphate created in RBC during glycolysis so when one is in a high altitude the number RBCs increased therefore increased hemoglobin and ______
2,3 BPG also known as 2,3DPG
elevated state of 2,3 BPG lowers affinity of HbA for 02 (increase P50) which enhances release of oxygen at the tissues
state of hemoglobin: __________-
T state (deoxyhemoglobin)
through _________- you will form carbonic acid
carbonic anhydrase
at lower pH, ________ is protonated which favors deoxyhemoglobin conformation thereby leading to release of oxygen
His 146
CO2 are carried to the lungs as _______- some are covalently bound to hemoglobin
bicarbonate
when hemoglobin combines with CO it forms a very bright red compound called ____
carboxyhemoglobin
hydrogen cyanide taken to the body’s tissues where it binds to an enzyme called ___________ and stops cells from being able to use oxygen
hydrogen cyanide
a right shift (decreased oxygen affinity) the P50 is higher can be caused by an increase in these factors:
4 factors stated
temperature
high protons
pCO2
red cell 2,3 BPG level
form of abnormal hemoglobin where ferrous which is normally found in hemoglobin is converted to the ferric state
methemoglobinemia
His F8 has been replaced by tyrosine
hemoglobin M
