Myoglobinuria historical perspective
Myoglobin was the first protein to have its three-dimensional structure revealed by X-ray crystallography.[1] This achievement was reported in 1958 by John Kendrew and associates.[2] For this discovery, John Kendrew shared the 1962 Nobel Prize in chemistry with Max Perutz.[3] Despite being one of the most studied proteins in biology, its physiological function is not yet conclusively established: mice genetically engineered to lack myoglobin can be viable and fertile but show many cellular and physiological adaptations to overcome the loss. Through observing these changes in myoglobin-deplete mice, it is hypothesised that myoglobin function relates to increased oxygen transport to muscle, oxygen storage and as a scavenger of reactive oxygen species.[4]
References
- ↑ (U.S.) National Science Foundation: Protein Data Bank Chronology (Jan. 21, 2004). Retrieved 3.17.2010
- ↑ Kendrew JC, Bodo G, Dintzis HM, Parrish RG, Wyckoff H, Phillips DC (Mar 1958). "A three-dimensional model of the myoglobin molecule obtained by x-ray analysis". Nature. 181 (4610): 662–6. Bibcode:1958Natur.181..662K. doi:10.1038/181662a0. PMID 13517261.
- ↑ The Nobel Prize in Chemistry 1962
- ↑ Garry DJ, Kanatous SB, Mammen PP (2007). "Molecular insights into the functional role of myoglobin". Advances in Experimental Medicine and Biology. 618: 181–93. doi:10.1007/978-0-387-75434-5_14. PMID 18269197.