Structure of bacterial luciferase

Curr Opin Struct Biol. 1995 Dec;5(6):798-809. doi: 10.1016/0959-440x(95)80014-x.

Abstract

The generation of light by living organisms such as fireflies, glow-worms, mushrooms, fish, or bacteria growing on decaying materials has been a subject of fascination throughout the ages, partly because it occurs without the need for high temperatures. The chemistry behind the numerous bioluminescent systems is quite varied, and the enzymes that catalyze the reactions, the luciferases, are a large and evolutionarily diverse group. The structure of the best understood of these intriguing enzymes, bacterial luciferase, has recently been determined, allowing discussion of features of the protein in structural terms for the first time.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Bacteria / enzymology*
  • Binding Sites
  • Flavin Mononucleotide / metabolism
  • Hydrogen Bonding
  • Kinetics
  • Luciferases / chemistry*
  • Luciferases / genetics
  • Luciferases / metabolism*
  • Luminescent Measurements
  • Models, Molecular
  • Oxygen / metabolism
  • Protein Conformation
  • Protein Folding
  • Protein Structure, Secondary

Substances

  • Flavin Mononucleotide
  • Luciferases
  • Oxygen