Interactions of long-chain aldehydes with luciferase. A carbon-13 nuclear magnetic resonance study

Biochemistry. 1979 Jun 12;18(12):2504-8. doi: 10.1021/bi00579a011.


The interaction of long-chain aldehydes with bacterial luciferase has been studied by 13C NMR spectroscopy of natural-abundance and 13C-enriched 1-dodecanal. At high substrate/enzyme ratios, the spin-spin relaxation rates of C(1)-C(3) are faster than for the other carbons and are in the order C(1) greater than C(2) greater than C(3). The aldehyde is strongly bound in the active site along the entire length of the alkyl chain with the strongest interaction at the CHO group. At low substrate/enzyme ratios, interactions are apparent at C(10), which are removed upon denaturation of the enzyme. Spin-spin and spin-lattice relaxation rates were measured for odd-carbon 13C-enriched 1-dodecanal in the presence of luciferase. From the ratios of T1/T2 a single value of (1.8 +/- 0.7) X 10(-8) s was calculated for the rotational correlation time tc for the complex.

MeSH terms

  • Aldehydes*
  • Luciferases*
  • Magnetic Resonance Spectroscopy
  • Mathematics
  • Protein Binding
  • Vibrio / enzymology


  • Aldehydes
  • Luciferases