Myoglobin haemoglobin

There has been extensive work done on myoglobin, haemoglobin, Cytocln-ome-c, rhodopsin and bacteriorhodopsin. In fact, there are literally hundreds of articles on each of the above subjects. Flere we will consider haemoglobin [12]. The first tliree of these examples are based on the protohaeme unit, shown in figure Bl.2.10. 

The primary structure of a large number of proteins is now known. They include ribonuclease, cytochrome c, myoglobin, haemoglobin, collagen, an amelogenin and lysozyme as well as various proteolytic enzymes, such as trypsin, chymotrypsin and pepsin and the single chain of human serum albumin which contains 582 residues. 

Figure Bl.2.10. Structure of the protohaeme unit found in haemoglobin and myoglobin.

Figure Bl.2.11. Biologically active centre in myoglobin or one of the subunits of haemoglobin. The bound CO molecule as well as the proximal and distal histidines are shown m addition to the protohaeme unit. From Rousseau D L and Friedman J M 1988 Biological Applications of Raman Spectroscopy vol 3, ed T G Spiro (New York Wiley). Reprinted by pennission of John Wiley and Sons Inc.

Fermi, G., Pemtz, M.F. Atlas of Molecular Structures in Biology. 2. Haemoglobin and Myoglobin. Oxford,... 

The 4 g of iron in the human body is normally com-partmented into its functional locations in the haem- and non-haem-containing, and iron-binding proteins and enzymes (Fig. 3.5). The majority (65%) of the iron is in the divalent state in haemoglobin and myoglobin, which are involved in the transport and storage of oxygen in erythrocytes and myocytes, respectively. The remainder is distributed between storage sites, predominantly in the... 

Hard, S. and Kanner, J. (1989). Haemoglobin and myoglobin as inhibitors of hydroxyl radical generation in a model system of iron redox cycle. Free Rad. Res. Commun, 6, 1-10. 

D. Mimica, J.H. Zagal, and F. Bedioui, Electroreduction of nitrite by hemin, myoglobin and haemoglobin in surfactant films. J. Electroanal. Chem. 497, 106-113 (2001). 

J. Ye and R.P. Baldwin, Catalytic reduction of myoglobin and haemoglobin at chemically modified electrodes containing methylene blue. Anal. Chem. 60, 2263—2268 (1988). 

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