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Title: sup 15 N NMR study on cyanide (C sup 15 N sup minus ) complex of cytochrome P-450 sub cam. Effects of d-camphor and putidaredoxin on the iron-ligand structure

Journal Article · · Journal of the American Chemical Society; (USA)
DOI:https://doi.org/10.1021/ja00202a007· OSTI ID:6719831
;  [1]; ;  [2];  [3]
  1. Institute of Physical and Chemical Research, Saitama (Japan)
  2. Keio Univ., Tokyo (Japan)
  3. Kyoto Univ. (Japan)

The cyanide (C{sup 15}N{sup {minus}}) complex of Pseudomonas putida cytochrome P-450 (P-450{sub cam}) exhibited well-resolved and hyperfine-shifted {sup 15}N NMR resonances arising from the iron-bound C{sup 15}N{sup {minus}} at 423 and 500 ppm in the absence and presence of the substrate, d-camphor, respectively. The values were smaller than those for cyanide complexes of myoglobin and hemoglobin ({approx} 1000 ppm) but fell into the same range as those for the cyanide complexes of peroxidases ({approx} 500 ppm). The {sup 15}N shift values of P-450{sub cam} were not incompatible with the existence of anionic ligand, such as cysteinyl thiolate anion, at the fifth coordination site of heme iron. The difference in the {sup 15}N chemical shift values between camphor-free and bound enzymes was inferred by the increase in the steric constraint to the Fe-C-N bond upon substrate binding.

OSTI ID:
6719831
Journal Information:
Journal of the American Chemical Society; (USA), Vol. 111:20; ISSN 0002-7863
Country of Publication:
United States
Language:
English