CHEMISTRY OF RESPIRATION

Question 1

heme proteins that maintain a supply of oxygen essential for oxidative metabolism

Answer 1

myoglobin
hemoglobin

Question 2

myoglobin is rich in ____ helices

Answer 2

alpha helices

Question 3

5th coordination position of iron is linked to a ring nitrogen

Answer 3

proximal histidine / His F8

Question 4

lies on the side of the heme ring opposite to His F8

Answer 4

Distal Histidine/ His E7

Question 5

___________ provides a hindered environment for heme iron

Answer 5

apomyoglobin

Question 6

the distal E7 histidine hinders bonding of carbon dioxide at the preferred _______ angle to the plane of the heme ring

Answer 6

90 degree

Question 7

in oxygenation of myoglobin accompanied motion of the iron, _______ and of residues linked to _______

Answer 7

His F8

Question 8

a tetrameric protein of erythrocytes

transports oxygen to tissues and returns carbon dioxide and protons to the lungs

Answer 8

hemoglobin

Question 9

hemoglobins bind ____ molecules of oxygen per tetramer one per heme

Answer 9

4

Question 10

hemoglobin has a ________curve

Answer 10

sigmoid

Question 11

myoglobin has a __________ curve

Answer 11

hyperbolic curve

Question 12

iron is not aligned with the heme plane

in the 6th coordination position of iron, it is not bound to oxygen yet

Answer 12

T state

Question 13

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

Answer 13

R state oxyhemoglobin

Question 14

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

Answer 14

cooperative tissues

Question 15

__________ is an organophosphate created in RBC during glycolysis so when one is in a high altitude the number RBCs increased therefore increased hemoglobin and ______

Answer 15

2,3 BPG also known as 2,3DPG

Question 16

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: __________-

Answer 16

T state (deoxyhemoglobin)

Question 17

through _________- you will form carbonic acid

Answer 17

carbonic anhydrase

Question 18

at lower pH, ________ is protonated which favors deoxyhemoglobin conformation thereby leading to release of oxygen

Answer 18

His 146

Question 19

CO2 are carried to the lungs as _______- some are covalently bound to hemoglobin

Answer 19

bicarbonate

Question 20

when hemoglobin combines with CO it forms a very bright red compound called ____

Answer 20

carboxyhemoglobin

Question 21

hydrogen cyanide taken to the body’s tissues where it binds to an enzyme called ___________ and stops cells from being able to use oxygen

Answer 21

hydrogen cyanide

Question 22

a right shift (decreased oxygen affinity) the P50 is higher can be caused by an increase in these factors:

4 factors stated

Answer 22

temperature
high protons
pCO2
red cell 2,3 BPG level

Question 23

form of abnormal hemoglobin where ferrous which is normally found in hemoglobin is converted to the ferric state

Answer 23

methemoglobinemia

Question 24

His F8 has been replaced by tyrosine

Answer 24

hemoglobin M

Question 25

mutations that favor R state increase oxygen affinity

Answer 25

HB Chesapeake

Question 26

most common type of abnormal hemoglobin

a valine replaced a glutamic acid in the 6th position of the beta chain of globin

Answer 26

sickle cell anemia

Question 27

point mutation resulting in abnormality in beta globin synthesis

Answer 27

beta thalassemia

Question 28

deletion mutation resulting in abnormality in aplha globin synthesis

Answer 28

alpha thalassemia