[MYG_PHYMC] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
Evolutionary Conservation
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Publication Abstract from PubMed
We have determined eight X-ray structures of myoglobin mutant L29W at various experimental conditions. In addition, infrared spectroscopic experiments are presented, which are discussed in the light of the X-ray structures. Two distinct conformations of the CO-ligated protein were identified, giving rise to two stretching bands of heme-bound CO. If L29W MbCO crystals are illuminated around 180 K, a deoxy species is formed. The CO molecules migrate to the proximal side of the heme and remain trapped in the so-called Xe1 cavity upon temperature decrease to 105 K. The structure of this photoproduct is almost identical to the equilibrium high-temperature deoxy Mb structure. If the temperature is cycled to increasingly higher values, CO recombination is observed. Three intermediate structures have been determined during the rebinding process. Efficient recombination occurs only above 180 K, the characteristic temperature for the onset of protein dynamics. Rebinding is remarkably slow because bulky residues His64 and Trp29 block important migration pathways of the CO molecule.
Ligand migration and protein fluctuations in myoglobin mutant L29W.,Nienhaus K, Ostermann A, Nienhaus GU, Parak FG, Schmidt M Biochemistry. 2005 Apr 5;44(13):5095-105. PMID:15794647[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑Nienhaus K, Ostermann A, Nienhaus GU, Parak FG, Schmidt M. Ligand migration and protein fluctuations in myoglobin mutant L29W. Biochemistry. 2005 Apr 5;44(13):5095-105. PMID:15794647 doi:10.1021/bi047513t
