In hemoglobin

Owrutsky J C, Li M, Locke B and Hochstrasser R M 1995 Vibrational relaxation of the CO stretch vibration in hemoglobin-CO, myoglobin-CO, and protoheme-CO J. Rhys. Chem. 99 4842-6... 

Genberg L, Richard L, McLendon G and Miller R J D 1991 Direct observation of global protein motion in hemoglobin and myoglobin on picosecond time scales Science 251 1051-6... 

Friedman J M 1994 Time-resolved resonance Raman spectroscopy as probe of structure, dynamics, and reactivity in hemoglobin Methods Enzymol. 232 205-31... 

Nevertheless, the technique suffers from a severe time scale problem -the trajectories are computed for (at most) a few nanoseconds. This is far too short compared to times required for many processes in biophysics. For example, the ii to T conformational transition in hemoglobin lasts tens of microseconds [1], and the typical time for ion migration through the gramicidin channel is hundreds of nanoseconds. This limits (of course) our ability to make a meaningful comparison to experiments, using MD. 

Iron is a vital constituent of plant and animal life and appears in hemoglobin. 

It is proposed to polymerize the vinyl group of the hemin molecule with other vinyl comonomers to prepare model compounds to be used in hemoglobin research. Considering hemin and styrene to be species 1 and 2, respectively, use the resonance concept to rank the reactivity ratios rj and X2. 

Iron is indispensable in the human body (see Mineral nutrients). The average adult body contains 3 grams of iron. About 65% is found in hemoglobin, which carries oxygen from the lungs to the various parts of the body. Iron is also needed for the proper functioning of cells, muscles, and other tissues (4). 

The allosteric effect is seen in hemoglobin which can exist in two quaternary stmctural states oxygenated (R) or deoxygenated (T). The binding of one O2 or some other effector to one of the subunits stabilizes the R form as compared to the T form. Binding of a second and third O2 stabilizes it even further. 

Aperture impedance measurements of cell volume must take into account the osmolaUty and pH of the medium. A hypotonic medium causes cells to swell a hypertonic medium causes them to shrink. Some manufacturers of aperture impedance counters deHberately provide hypertonic electrolytic media for red blood cell measurements. The shmnken red cells not only become more nearly spherical and thus less affected by orientation, but also less deformable than cells in isotonic media and thus less affected by differences in hemoglobin content. 

Proteins may consist exclusively of a polymeric chain of amino acids these are the simple proteins. Quite often some other chemical component is covalendy bonded to the amino acid chain. Glycoproteins and Hpoproteins contain sugar and Hpid components, respectively. Porphyrins are frequently associated with proteins, eg, in hemoglobin. Proteins bound to other chemical components are called conjugated proteins. Most enzymes are conjugated proteins. 

The most conspicuous use of iron in biological systems is in our blood, where the erythrocytes are filled with the oxygen-binding protein hemoglobin. The red color of blood is due to the iron atom bound to the heme group in hemoglobin. Similar heme-bound iron atoms are present in a number of proteins involved in electron-transfer reactions, notably cytochromes. A chemically more sophisticated use of iron is found in an enzyme, ribo nucleotide reductase, that catalyzes the conversion of ribonucleotides to deoxyribonucleotides, an important step in the synthesis of the building blocks of DNA. 

Movement of the Heme Iron hy Less Than 0.04 nm Induces the Conformational Change in Hemoglobin... 

FIGURE 15.31 Subunit motion in hemoglobin when the molecule goes from the (a) deoxy to the (b) oxy form. (Irving G sj... 

FIGURE 15.33 Salt bridges between different subunits in hemoglobin. These noncova-... 

Cytochromes were first named and classified on the basis of their absorption spectra (Figure 21.9), which depend upon the structure and environment of their heme groups. The b cytochromes contain iron—protoporphyrin IX (Figure 21.10), the same heme found in hemoglobin and myoglobin. The c cytochromes contain heme c, derived from iron-protoporphyrin IX by the covalent attachment of cysteine residues from the associated protein. UQ-cyt c... 

Porphyrins, derivatives of porphin, are best known for their role as oxygen earriers in hemoglobin. 

The amino acid sequence in hemoglobin, with 574 units, is known. 

Manz, B Stilbs, P Jonsson, B Soderman, O Callaghan, PT, NMR Imaging of the Time Evolution of Electroosmotic Flow in a Capillary, Journal of Physical Chemistry 99, 11297, 1995. Matthew, JB Hanania, GIH Gurd, FRN, Electrostatic Effects in Hemoglobin Bohr Effect and Ionic Strength Dependence of Individual Groups, Biochemistry 18, 1928, 1979. 

Matthew, JB Hanania, GIH Gurd, ERN, Electrostatic Effects in Hemoglobin Hydrogen Ion Equilibria in Human Deoxy- and Oxyhemoglobin A, Biochemistry 18, 1919, 1979. 

In hemoglobin M, histidine F8 (His F8) has been replaced by tyrosine. The iron of HbM forms a tight ionic complex with the phenolate anion of tyrosine that stabilizes the Fc3 form. In a-chain hemoglobin M variants, the R-T equilibrium favors the T state. Oxygen affinity is reduced, and the Bohr effect is absent. P Ghain hemoglobin M variants exhibit R-T switching, and the Bohr effect is therefore present. 

Manning JM et aJ Normal and abnormal protein subunit interactions in hemoglobins.] Biol Chem 1998 273 19359-Mario N, Baudin B, Giboudeau J Qualitative and quantitative analysis of hemoglobin variants by capillary isoelectric focusing. J Chromatogr B Biomed Sci Appl 1998 706 123-Reed W, Vichinsky EP New considerations in the treatment of sickle cell disease. Annu Rev Med 1998 49 46l. 

---