O2 Binding Properties of Human Serum Albumin Quadruple Mutant Complexed Iron Protoporphyrin IX with Axial His-186 Coordination
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[1] S. Curry,et al. Genetic engineering of the heme pocket in human serum albumin: modulation of O2 binding of iron protoporphyrin IX by variation of distal amino acids. , 2007, Journal of the American Chemical Society.
[2] S. Curry,et al. O2 and CO binding properties of artificial hemoproteins formed by complexing iron protoporphyrin IX with human serum albumin mutants. , 2005, Journal of the American Chemical Society.
[3] S. Curry,et al. Dioxygenation of human serum albumin having a prosthetic heme group in a tailor-made heme pocket. , 2004, Journal of the American Chemical Society.
[4] Eishun Tsuchida,et al. BMC Structural Biology BioMed Central , 2003 .
[5] D. Carter,et al. The atomic structure of human methemalbumin at 1.9 A. , 2002, Biochemical and biophysical research communications.
[6] S. Sligar,et al. The effects of amino acid substitution at position E7 (residue 64) on the kinetics of ligand binding to sperm whale myoglobin. , 1990, The Journal of biological chemistry.
[7] J. Cannon,et al. Syntheses and NMR characterization of chelated heme models of hemoproteins , 1979 .
[8] Q. Gibson,et al. The dissociation of the first oxygen molecule from some mammalian oxyhemoglobins. , 1971, The Journal of biological chemistry.
[9] Q. Gibson. The reaction of oxygen with hemoglobin and the kinetic basis of the effect of salt on binding of oxygen. , 1970, Journal of Biological Chemistry.
[10] K. Imai,et al. Studies on the function of abnormal hemoglobins. I. An improved method for automatic measurement of the oxygen equilibrium curve of hemoglobin. , 1970, Biochimica et biophysica acta.