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Structural features of the protophorphyrin-apomyoglobin complex. A proton NMR spectroscopy study

Journal Article · · Biochemistry; (USA)
DOI:https://doi.org/10.1021/bi00502a007· OSTI ID:5526406
;  [1]
  1. The Pennsylvania State Univ., University Park (USA)

The structural properties of the complex formed by apomyoglobin and protoporphyrin IX (des-iron myoglobin) were studied to probe the influence of iron-to-histidine coordination on the native myoglobin fold and the heme binding site geometry. Standard two-dimensional proton nuclear magnetic resonance spectroscopy methods were applied to identify porphyrin and protein signals. A pronounced spectral resemblance between carbonmonoxymyoglobin and des-iron myogobin was noticed that could be exploited to assign a number of resonances by nuclear Overhauser spectroscopy. Protoporphyrin IX was determined to bind in the same orientation as the heme. Most residues in contact with the prosthetic group were found in the holomyoglobin conformation. Several tertiary structure features were also characterized near the protein termini. It was concluded that the protoporphyrin-apomyoglobin interactions are capable of organizing the binding site and the unfolded region of the apoprotein into the native holoprotein structure.

OSTI ID:
5526406
Journal Information:
Biochemistry; (USA), Journal Name: Biochemistry; (USA) Vol. 29:50; ISSN 0006-2960; ISSN BICHA
Country of Publication:
United States
Language:
English