Heme Oxygenase The Protein

Heme oxygenase HO-2 has been partially purified from rat testes and the full-length protein has been expressed in an active form in E. coli (11, 61-63). Truncation of the protein at the C-terminus provides 

Although more limited, sufficient spectroscopic data is available on the HO-2 isoform to confirm that the proximal ligand is also an imidazole. A 28-kDa catalytically active fragment of human HO-2 obtained by tryptic digestion of the enz5mie expressed in E. coli was shown by optical, resonance Raman, and EPR studies to have a neutral (imionized) 

Mutation of His 132 to an alanine, glycine, or serine in the truncated human heme oxygenase, in accord with identification of His25 as the proximal ligand, does not alter the cpe-His band in the resonance Raman spectrum of the Fe deoxy protein (82). The mutations result in the formation of two separate fractions when the protein is expressed in 

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Biological Function of Heme Oxygenase Heme Oxygenase Model Systems Heme Oxygenase The Protein... 

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