MSN 6050 Module 3 Quiz

What is significant about the heme structure in hemeproteins? 

• Allows for transition between ferrous (Fe2+) and ferric (Fe3+) states

• Can form larger complexes

• Interior is nearly entirely nonpolar, and exterior is nearly all polar R-groups

• Iron is held in the center by four nitrogen atoms of the ring

• both A and D

Myoglobin and hemoglobin are globular proteins

• True

• False

____________protein is found in abundance in the heart and skeletal muscle, involved in oxygen transport in muscle tissues. 

__________ protein is exclusive to erythrocytes (red blood cells) to transport oxygen from the lungs to tissues of the body through the circulatory system 

Myoglobin has one heme, so can only bind one O2. 

• True

• False

Which is not an allosteric regulator of hemoglobin? 

• [2,3-bisphosphoglycerate (BPG)]

• pH of environment

• reversible binding ability

• pH of environment

The____________ reflects the fact that the deoxy form of hemoglobin has a greater affinity for protons than does oxyhemoglobin

______________ is a point mutation changes an amino acid in the β-globin chain from Glu to Val.

We consume iron in the ferric (oxidized) form, but it has to be converted to the ferrous (reduced) form

• True

• False

Which form of iron is needed for heme and hemoglobin synthesis ? Ferrous or ferric?