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 inCurrent opinion in structural biology Vol. 5; no. 6; pp. 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 Journal Article
LanguageEnglish
Published England Elsevier Ltd 01.12.1995
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
FMN—flavin mononucleotide
YFP—yellow fluorescent protein
TIM—triose-phosphate isomerase
Online AccessGet full text

Cover

More Information
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.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
ObjectType-Review-3
content type line 23
ObjectType-Article-1
ObjectType-Feature-2
ISSN:0959-440X
1879-033X
DOI:10.1016/0959-440X(95)80014-X