Crystallographic investigations of the tryptophan-derived cofactor in the quinoprotein methylamine dehydrogenase

A model of tryptophan tryptophylquinone (TTQ), recently proposed by Mclntire et al. (Science (1991) 252, 817-824) to be the prosthetic group of the quinoprotein methylamine dehydrogenase, has been compared with electron density maps of this dehydrogenase from Thiobacillus versutus and Paracoccus den...

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Bibliographic Details
Published in:FEBS letters 1991-08, Vol.287 (1), p.163-166
Main Authors: Chen, Longyin, Mathews, F.Scott, Davidson, Victor L., Huizinga, Eric G., Vellieux, Frederic M.D., Duine, Johannis A., Hol, Wim G.J.
Format: Article
Language:English
Subjects:
Amino acid-derived cofactor
Analytical, structural and metabolic biochemistry
Binding Sites
Biological and medical sciences
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Hydrogen Bonding
Indolequinones
Macromolecular Substances
Methylamine dehydrogenase
Models, Molecular
Molecular Structure
Oxidation-Reduction
Oxidoreductases
Oxidoreductases Acting on CH-NH Group Donors - chemistry
Paracoccus denitrificans
Paracoccus denitrificans - enzymology
Pyrroloquinoline quinone
Quinones - chemistry
Quinoprotein
Redox cofactor
Thiobacillus - enzymology
Thiobacillus versutus
Tryptophan - analogs & derivatives
Tryptophan - chemistry
Tryptophan tryptophylquinone
X-Ray Diffraction
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Summary:A model of tryptophan tryptophylquinone (TTQ), recently proposed by Mclntire et al. (Science (1991) 252, 817-824) to be the prosthetic group of the quinoprotein methylamine dehydrogenase, has been compared with electron density maps of this dehydrogenase from Thiobacillus versutus and Paracoccus denitrificans. The comparison shows that the TTQ model can be neatly accommodated, providing strong supportive evidence that TTQ is indeed the cofactor for this group of quinoproteins.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(91)80041-Z