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1
-
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3543098900
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note
-
Abbreviations used: hHO, human heme oxygenase-1; rHO, rat heme oxygenase-1; HO-1, heme oxygenase isoform 1; TOCSY, 2D total correlation spectroscopy; NOESY, 2D nuclear Overhauser spectroscopy; Mb, myoglobin; PH, protohemin IX; WEFT, water-eliminated Fourier transform.
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33
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3543053141
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note
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18 exhibits spectroscopic and catalytic properties similar to those of the wild-type enzyme. His 132 thus appears not to be a critical catalytic residue.
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35
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note
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Four additional, inconsequentially relaxed, partially resolved labile protons in the 10-12-ppm window similarly are involved in H-bond interactions which are pairwise pseudosymmetric in shifts and dipolar contacts (not shown). The nature of these pseudosymmetric H-bond interactions is not known, but since at least one of these residues, His 132, is completely conserved, it is likely that the interactions are important in stabilizing the structure required for catalysis.
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51
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3543123199
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-
note
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αH with a strong, low-field shift even in diamagnetic hHO, and hence can be assumed to represent the same residue. Similar comparison between hHO and hHO-PH-CN for other aromatic rings failed to provide any additional convincing correlations.
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