Structure of bacterial luciferase

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 bioluminesce...

Full description

Saved in:
Bibliographic Details
Published in:Current opinion in structural biology 1995-12, Vol.5 (6), p.798-809
Main Authors: Baldwin, Thomas O, Christopher, Jon A, Raushel, Frank M, Sinclair, James F, Ziegler, Miriam M, Fisher, Andrew J, Rayment, Ivan
Format: Article
Language:English
Subjects:
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
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:0959-440X
1879-033X
DOI:10.1016/0959-440X(95)80014-X