State of configuration. Classically, the T form of the protein is less active,whereas the R form is more active.As we shall see, this phenomenon of allosterism allows for efficient and multiple ways of regulating the ability of a protein to bind a ligand and to become either more active (R form) or less active (T form). Those ligands that bind to the protein or to an enzyme toenhance its function are known as positive allosteric effectors, whereas those that bind tocause a decreased level of functional are referred to as negative allosteric effectors.
Structure of Hemoglobin (Hb)
When the metabolic pathways associated with aerobic respiration began to appear, so didthe ability of cells to produce great sums of additional energy, compared to the relativelysmall amount of ATP that could be generated from anaerobic respiration. With higher levels of energy production, greater and greater molecular-genetic variability could besupported, and a huge leap in specialized cellular activity could be realized. However, asystem had to be available to deliver that insoluble oxygen to the tissues for aerobicrespiration. The molecular and cellular environment within the erythrocyte provided justwhat was needed for delivering oxygen from the lungs to the tissues, within the contextof the circulatory system. Within this intra-erythrocytic environment, wherein there areneither nuclei nor mitochondria, are found the well described hemoglobin molecules ingreat quantity plus an effective bicarbonate buffer system, which we shall discuss shortlyin detail. The erythrocyte is the only cell that contains hemoglobin.The primary function of hemoglobin is to transfer oxygen from the lungs to the tissues. Itis a tetrameric, heme protein that is comprised of four subunits (hence tetrameric), twoidentical
subunits and two identical
Hb has quarternarystructure (remember, quarternary refers to a protein having two or more subunits). Boththe
- and the
-subunits are structurally related to one another and to the single subunitmolecule, myoglobin (which we discuss later in this lecture), even though only about18% of the amino acids are identical in the twp types of subunits.
Each α-subunit iscomprised of 141 amino acids, whereas each β-subunit is composed of 146. About 75% of the complete structure of hemoglobin comprised of these four subunits is in the form of the α-helix.
Within the center of eachof the four subunits is a heme molecule, which is a protoporphyrin ring structure with aniron atom in the center.
Familiarize yourself with the heme structure, shown on page355 of your text, for the second exam.
Below is a ribbon diagram of the hemoglobinmolecule showing the four subunits, each in a different color and with each containing aheme molecule. As you observe the diagram,
consider why each subunit fulfills thecriteria of having tertiary structure (review those criteria from last week)
and howthe bonding of those subunits forms a quaternary protein structure.