1. Gros, G., Wittenberg, A. B., and Jue, T. (2010) Myoglobin old and new clothes: from molecular structure to function in living cells, J. Exp. Biol., 213, 2713–2725.
2. Atanasov, B. P., and Zhizheskaia, G. Ia. (1975) Acid-alkaline equilibrium of the ferri-leghemoglobin of the lupine (Lupinus luteus L.). Spectral studies, Mol. Biol. (Moscow), 9, 491–501.
3. Krasnobaeva, N. N., and Atanasov, B. P. (1978) Lupine leghemoglobin affinity to ligands. The effect of pH and buffer nature, Mol. Biol. (Moscow), 12, 1239–1245.
4. Fuchsman, W. H., and Appleby, C. A. (1979) CO and O2 complexes of soybean leghemoglobin: pH effects upon infrared and visible spectra. Comparisons with CO and of myoglobin and hemoglobin, Biochemistry, 18, 1309–1321.
5. Voet, D., and Voet, G. J. (2008) Fundamentals of Biochemistry, 3rd Edn., John Wiley & Sons.