NMR studies of strong hydrogen bonds in enzymes and in a model compound

T. K. Harris, Q. Zhao, A. S. Mildvan

Research output: Contribution to journalArticle

48 Scopus citations

Abstract

Hydrogen bond lengths on enzymes have been derived with high precision (≤ ± 0.05 Å) from both the proton chemical shifts (δ) and the fractionation factors (φ) of the proton involved and were compared with those obtained from protein X-ray crystallography. Hydrogen bond lengths derived from proton chemical shifts were obtained from a correlation of 59 O-H···O hydrogen bond lengths, measured by small molecule high resolution X-ray crystallography, with chemical shifts determined by solid-state NMR in the same crystals [A. McDermott, C.F. Ridenour, Encyclopedia of NMR, Wiley, Sussex, England, 1996, 3820pp]. Hydrogen bond lengths were independently obtained from fractionation factors which yield distances between the two proton wells in quartic double minimum potential functions [M.M. Kreevoy, T.M. Liang, J. Am. Chem. Soc. 102 (1980) 3315]. The high precision hydrogen bond lengths derived from their corresponding NMR-measured proton chemical shifts and fractionation factors agree well with each other and with those reported in protein X-ray structures within the larger errors (±0.2-0.8 Å) in lengths obtained by protein X-ray crystallography. The increased precision in measurements of hydrogen bond lengths by NMR has provided insight into the contributions of short, strong hydrogen bonds to catalysis for several enzymes including ketosteroid isomerase, triosephosphate isomerase, and serine proteases. The O-H···O hydrogen bond length derived from the proton chemical shift in a model dihydroxy-naphthalene compound in aqueous solution agreed well with lengths of such hydrogen bonds determined by high resolution, small molecule X-ray diffraction. (C) 2000 Elsevier Science B.V.

Original languageEnglish (US)
Pages (from-to)97-109
Number of pages13
JournalJournal of Molecular Structure
Volume552
Issue number1-3
DOIs
StatePublished - Sep 26 2000
Externally publishedYes

Keywords

  • Chemical shift
  • Chymotrypsin
  • Chymotrypsinogen
  • Fractionation factor
  • Ketosteroid isomerase
  • Serine protease
  • Subtilisin
  • Triosephosphate isomerase

ASJC Scopus subject areas

  • Structural Biology
  • Organic Chemistry
  • Physical and Theoretical Chemistry
  • Spectroscopy
  • Atomic and Molecular Physics, and Optics

Fingerprint Dive into the research topics of 'NMR studies of strong hydrogen bonds in enzymes and in a model compound'. Together they form a unique fingerprint.

  • Cite this