Solution 1H NMR of the active site of substrate-bound, cyanide-inhibited human heme oxygenase. comparison to the crystal structure of the water-ligated form.
La Mar GN, Asokan A, Espiritu B, Yeh DC, Auclair K, Ortiz De Montellano PR.
La Mar GN, et al. Among authors: ortiz de montellano pr.
J Biol Chem. 2001 May 11;276(19):15676-87. doi: 10.1074/jbc.M009974200. Epub 2001 Jan 31.
J Biol Chem. 2001.
PMID: 11297521
Free article.
The majority of the active site residues of cyanide-inhibited, substrate-bound human heme oxygenase have been assigned on the basis of two-dimensional NMR using the crystal structure of the water-ligated substrate complex as a guide (Schuller, D. J., Wilks, A., Ortiz de …
The majority of the active site residues of cyanide-inhibited, substrate-bound human heme oxygenase have been assigned on the basis of two-d …