Assignment of heme and distal amino acid resonances in the 1H-NMR spectra of the carbon monoxide and oxygen complexes of sperm whale myoglobin

Bridget C. Mabbutt, Peter E. Wright*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

69 Citations (Scopus)

Abstract

Assignments of resonances of the heme and distal amino acid protons in spectra of the CO and O2 complexes of sperm whale myoglobin are reported. These resonances provide information on the conformation of the heme pocket. For oxymyoglobin, the assignments of the heme meso protons disagree with those proposed previously on the basis of partial deuteration experiments. Rapid ring flips about the Cβ-Cγ bond are detected for Phe-CD1. Recent claims for two conformational substrates of valine-E11 in carbonmonoxymyoglobin (Bradbury, J.H. and Carver, J.A. (1984) Biochemistry 23, 4905-4913) are shown to be in error. The pK of His-97 (FG3) in carbonmonoxymyoglobin has been determined (pK = 5.9). This residue appears to influence many spectroscopic properties of myoglobin. The distal His-E7 in carbonmonoxymyoglobin has pK < 5.0. Differences in the heme pocket conformation in the CO complexes of myoglobin and leghemoglobin are discussed. These differences may be influential in O2 and CO association reactions.

Original languageEnglish
Pages (from-to)175-185
Number of pages11
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume832
Issue number2
DOIs
Publication statusPublished - 29 Nov 1985
Externally publishedYes

Keywords

  • (Sperm whale)
  • Amino acid
  • Heme group
  • Myoglobin
  • NMR
  • Resonance assignment

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