Research on structure, mechanism and regulation of enzyme activity. Works of Nobel laureates C. Anfinsen, S. Moore, W. Stein, S. Prusiner, J. Skou, P. Boyer, J. Walker

Abstract

Although the protein nature of enzymes was identified in the 40s of the 20th century, (we wrote about this in our previous article), their molecular structure and the specific mechanism of action remained unknown. Researchers of the next generations faced the challenges and a major breakthrough was achieved. In 1960, American biochemists S. Moore and W. Stein determined the complete amino acid sequence of enzyme ribonuclease. It was one of the first proteins and the first enzyme whose primary structure was established. In 1972, for this discovery, they received the Nobel Prize in Chemistry jointly to Christian Anfinsen who worked on the same problem. Works of Nobel Laureates in Chemistry in 1997 – Jens Christian Skou (for the discovery of the Na+,K+-activated ATPase), Paul Boyer and John Walker (for the discovery of the mechanism of action of H+-ATP synthase – the most important enzyme for bioenergy) were a huge step forward in the deciphering the mechanisms of enzyme action. The second half of the 20th century was marked by another outstanding discovery in the field of biology and medicine – the identification and characterization of prions – the proteins that cause neurodegenerative spongiform encephalopathies in humans and animals. For this work, American biochemist Stanley B. Prusiner received the Nobel Prize in Physiology or Medicine in 1997. This discovery is of great theoretical significance for biochemical science. The development of new research methods and technological advances formed the basis for significant scientific achievements in this field of biochemistry and molecular biology. This was the golden era of protein chemistry.

Keywords

• c. anfinsen
• s. moore
• w. stein
• s. prusiner
• j. skou
• p. boyer
• j. walker
• ribonuclease
• na(+);k(+)-activated atpase
• h(+)-atp synthase
• prions