Myoglobins chemistry

For their work on myoglobin and hemoglobin respec tively John C Kendrew and Max F Perutz were awarded the 1962 Nobel Prize in chemistry... 

The first four materials (IRMM/IFCC-452, 453, 454, 455) are expected to be released during 2000. Projects on the certification of reference materials for cardiac marker (myoglobin) and total protein concentration in serum are under discussion. Even so the number of available CRMs for clinical chemistry and occupational toxicology is still limited. This has to do with the complexity of physiological compounds (e.g. proteins), the instabihty (e.g. enzymes), or the volatility (e.g. solvents). 

Blaxter, M.L., Vanfleteren, J., Xia, J. and Moens, L. (1994b) Structural characterisation of an Ascaris myoglobin. Journal of Biological Chemistry 269, 30181-30186. 

A brief look at the contents page of any recent issue of the Journal of Molecular Biology (founded by John Kendrew, protein crystallographer and winner of the Nobel Prize for Chemistry together with Max Perutz for the 3-D structures of myoglobin and haemoglobin) will clearly establish that this is not so. 

Taken together with the temperature dependence of the x ) values, this study of the thermal expansion of myoglobin provides the most detailed picture yet available of the physical chemistry of a protein. It... 

Interest in the chemistry of myoglobin originated many decades ago and has led to recognition that the environment provided to the heme... 

Peroxidases and catalases contain high-spin Fe(III) and resemble metmyoglobin in properties. The enzymes are reducible to the Fe(II) state in which form they are able to combine (irreversibly) with 02. We see that the same active center found in myoglobin and hemoglobin is present but its chemistry has been modified by the proteins. The affinity for 02 has been altered drastically and a new group of catalytic activities for ferriheme-containing proteins has emerged. 

The elucidation of the structure of ribonuclcasc follows that of lycozyme by a group at London s Royal Institute headed by Dr. David C. Phillips, and that of the other protein, myoglobin, for which Dr. Max F. Perutz and Dr. John C. Kendrew of Cambridge University received the Nobel Prize in chemistry in 1962. 

PERUTZ. MAX F. (1914-2002). An Austrian molecular biologist and recipient of the Nobel prize for chemistry in 1962 along with John C. Kendrew, His work was concerned with crystalline protein structure, particularly the molecular structure of hemoglobin and myoglobin. His education was in England and Austria. 

In 1926, James B. Sumner, an American chemist, showed that enzymes were pure proteins and that enzymes could be crystallized. The fact that pure proteins could be enzymes was definitively proven by John H. Northrop and Wendell M. Stanley, who worked on digestive enzymes. Summer, Northrop, and Stanley were awarded the 1946 Nobel Prize in Chemistry for their work. The discovery that enzyme crystals could be grown eventually allowed their actual 3-D structures to be determined by X-ray crystallography. Myoglobin was the first protein to have its structure solved by X-ray crystallography by the British scientists Max Perutz and Sir John Kendrew in 1958. In 1959, Perutz also solved the structure of hemoglobin, which led to the two scientists sharing the 1962 Nobel Prize in Chemistry. 

One of the most significant common aspects of the chemistry of NO and peroxynitrite is their ability to react in a unique manner with the metal centers of numerous proteins, in particular hemoproteins [10]. We have used myoglobin (Mb) and hemoglobin (Hb) to investigate the diverse reactions that these simple inorganic biomolecules can undergo with different oxidation states of hemoproteins. Mutated forms of Mb and Hb are available [12, 13], and a large number of transition metals ions other than Fe ions have been successfully incorporated in these... 

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