Chapter 7 Hemoglobin:A Portrait of a Protein in Action 2 6 This type of hemoglobin is composed of two a chains and two y chains. Ans:k Section:7.2 7 This is the molecule whose function is to store oxygen is muscle cells. Ans:g Section:Introduction This oxidized hemeprotein does not reversibly bind oxygen. Ans:e Section:7.1 9 This type of binding is indicated by a sigmoidal-shaped binding curve. Ans:a Section:7.2 10 This condition is a result of a single point mutation in the B chain of hemoglobin. Ans:i Section:7.4 Fill in the Blank Questions 1 Under normal conditions,the heme iron in myoglobin and hemoglobin is in the oxidation state. Ans:ferrous,or Fe+2 Section:7.1 2 The ability of myoglobin to bind oxygen depends on the presence of a bound prosthetic group called Ans:heme Section:7.1 3 In hemoglobin,the iron of the heme is bonded to the four nitrogens of porphyrin and to the proximal residue of the globin chain. Ans:histidine Section:7.1 4 The binding of 2-3-bisphosphogycerate to hemoglobin (increases,decreases)its affinity of oxygen binding. Ans:decreases Section:7.2 5 The effect of pH on oxygen-binding of hemoglobin is referred to as the Ans:Bohr effect Section:7.3 6 Carbon dioxide reacts with the amino terminal groups of hemoglobin to form carbamate groups, which carry a. charge. Ans:negative Section:7.3Chapter 7 Hemoglobin: A Portrait of a Protein in Action 2 6 ____________ This type of hemoglobin is composed of two α chains and two γ chains. Ans: k Section: 7.2 7 ____________ This is the molecule whose function is to store oxygen is muscle cells. Ans: g Section: Introduction 8 ____________ This oxidized hemeprotein does not reversibly bind oxygen. Ans: e Section: 7.1 9 ____________ This type of binding is indicated by a sigmoidal-shaped binding curve. Ans: a Section: 7.2 10 ____________ This condition is a result of a single point mutation in the β chain of hemoglobin. Ans: i Section: 7.4 Fill in the Blank Questions 1 Under normal conditions, the heme iron in myoglobin and hemoglobin is in the ____________ oxidation state. Ans: ferrous, or Fe +2 Section: 7.1 2 The ability of myoglobin to bind oxygen depends on the presence of a bound prosthetic group called _____________. Ans: heme Section: 7.1 3 In hemoglobin, the iron of the heme is bonded to the four nitrogens of porphyrin and to the proximal ______________ residue of the globin chain. Ans: histidine Section: 7.1 4 The binding of 2-3-bisphosphogycerate to hemoglobin ____________ (increases, decreases) its affinity of oxygen binding. Ans: decreases Section: 7.2 5 The effect of pH on oxygen-binding of hemoglobin is referred to as the _____________. Ans: Bohr effect Section: 7.3 6 Carbon dioxide reacts with the amino terminal groups of hemoglobin to form carbamate groups, which carry a ______________ charge. Ans: negative Section: 7.3