Select all statements that correctly describe hemoglobin and myoglobin structure. By itself, heme is not a good oxygen carrier. It must be part of a larger protein to prevent oxidation of the iron. Molecular oxygen binds irreversibly to the Fe(II) atom in heme. Hemoglobin and myoglobin are heterotetramers. The heme prosthetic group is entirely buried within myoglobin. Each iron atom can form six coordination bonds. One of these bonds is formed between iron and oxygen. Each hemoglobin molecule can bind four oxygen molecules; each myoglobin can bind one oxygen molecule. Both hemoglobin and myoglobin contain a prosthetic group called heme, which contains a central iron (Fe) atom. 0000

Select the best answer or answers from the choices given: Oxygen and carbon dioxide are exchanged in the lungs and through all cell membranes by (a) active transport, (b) diffusion, (c) filtration, (d) osmosis.

What is the toxic form of oxygen? Why can this be toxic? Where/how is this toxic form made?

The primary and tertiary structures of hemoglobin and myoglobin are very similar and both contain the 'heme' group as an oxygen-binding prosthetic group. However this There are important functional differences between the two proteins. Hemoglobin oxygen transport protein, myoglobin functions as oxygen storage protein. Hemoglobin and consider the structural differences and oxygen binding curves between myoglobin why myoglobin is a good oxygen transport protein, while hemoglobin Explain why it cannot be a good oxygen storage protein.

What are the stages in carbon dioxide fixation (choose all that applies)? Conversion of unstable six-carbon compound to a stable five-carbon compound. Hydrolysis of enediolate intermediate to 3-phosphoglycerate and two molecules of CO2. Hydrolysis of unstable six-carbon compound to two molecules of 3-phosphoglycerate. Condensation of the CO2 molecule with the enediolate intermediate. Conversion of ribulose 1,5-bisphosphate into an enediolate intermediate.

I believe I use the diffusion law on this: (Diffusion Constant × ∆Concentration × Area) / Thickness. Then change the constant into micrometers (x10^-12). Maybe use the fact that oxygen = 16 grams/mol. Am I on the right track? Thank you for any help you can provide.

I now know the structure difference between myoglobin and hemoglobin , however which exctaly structure difference make myglobin become a oxygen storage ? and not a oxygen transport?? Be specific! details describe how the structure connect to their role. also which exctaly structure difference make hemoglobin become better oxygen transport?? I need the specific structure that contribute to their unique role.   I KNOW THE STRUCTURE DIFFERENCE , but don't understand which specific part make myoglobin only  bind to oxygen, and not release oxygen

There is a His residue labeled on the myoglobin structure below. What is that His residue commonly called? bound O, F helix His bound, to heme iron the conserved His residue. the hydrophobic His residue. the distal His residue. the proximal His residue. O None of the above is correct.

The classic demonstration that cell plasma membranes are composed ofbilayers depends on the following kinds of data:• The membrane lipids from 4.74 x 109erythrocytes will form a monolayer of area 0.89 m2when spread on a water surface.• The surface of one erythrocyte is approximately 100 μm2in area. Show that these data can be accounted for only if the erythrocyte membrane is a bilayer.

Which of the following would you not expect to find in a human erythrocyte? O Band 4.3 Spectrin Actin Glycophorin Smooth Endoplasmic Reticulum