Biology

Biology, 06.07.2019 06:20, bfell92

Which of the following statements is false? which of the following statements is false? myoglobin is a single polypeptide chain folded about a heme prosthetic group. hemoglobin is a tetramer, each of which binds a heme group. in both hemoglobin and myoglobin, iron is chelated by a tetrapyrole ring system. the iron in both hemoglobin and myoglobin has two coordination sites that bind to oxygen.

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Biology, 29.09.2019 20:30, joedawg50

Select the false statement below about the structure of myoglobin. a. the o2-binding pocket of myoglobin contains several nonpolar amino acid sidechains that can interact favorably with a nonpolar molecule of o2. b. the polypeptide of myoglobin provides a pocket for o2 to fit, and stabilizes the bound o2 via hydrogen bonding with the distal his. c. the polypeptide of myoglobin protects the heme iron from oxidation. d. the active site of deoxy myoglobin is 5-coordinate with a histidine occupying one axial position while the other axial position is left open for oxygen binding. e. myoglobin has a single polypeptide chain so it has 1o, 2o, 3o and 4o structure.

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Biology, 08.10.2019 03:00, cougs

Which five statements about hemoglobin and myoglobin structure are true? each iron atom can form six coordination bonds. two of these bonds are formed between iron and oxygen. hemoglobin is a heterotetramer, whereas myoglobin is a monomer. both hemoglobin and myoglobin contain a prosthetic group called heme, which contains a central iron atom. each hemoglobin or myoglobin molecule can bind four oxygen molecules. molecular oxygen binds reversibly to fe2+ in heme. by itself, heme is not a good oxygen carrier. it must be part of a larger protein to prevent oxidation of the iron atom. heme is composed of an organic protoporphyrin component and a metal atom.

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Chemistry, 16.10.2019 16:30, albusaidi4480

Identify the true statements regarding the heme group of myoglobin and hemoglobin. the iron in the heme group can form six bonds. the fifth is with an imidazole ring of a histidine, and the sixth is with oxygen. the globin chains of myoglobin and hemoglobin prevent the oxidation of fe2+fe2+ to fe3+fe3+ , which irreversibly binds oxygen. the cooperativity of oxygen binding in hemoglobin arises from a shorter fe−o2fe−o2 bond length in the t state compared to the r state. a heme group contains four pyrrole rings, which are linked via methene (methine) bridges. the heme group is conjugated. myoglobin contains one heme group. the r state of hemoglobin has greater affinity for o2o2 than the t state because the iron atom is in the plane of the porphyrin ring.

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Biology, 16.10.2019 21:20, jordanlacie65

Which five statements about hemoglobin and myoglobin structure are true? heme is composed of an organic protoporphyrin component and a metal atom. both hemoglobin and myoglobin contain a prosthetic group called heme, which contains a central iron atom. each hemoglobin molecule can bind four oxygen molecules; each myoglobin can bind only one oxygen molecule. hemoglobin and myoglobin are heterotetramers. each iron atom can form six coordination bonds. two of these bonds are formed between iron and oxygen. molecular oxygen binds reversibly to fe2+fe2+ in heme. by itself, heme is not a good oxygen carrier. it must be part of a larger protein to prevent oxidati

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