Crystallographic investigations of the tryptophan-derived cofactor in the quinoprotein methylamine dehydrogenase.
A model of tryptophan tryptophylquinone (TTQ), recently proposed by McIntire 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.
Chen
L Y
LY
Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, MO 63110.
Mathews
F S
FS
Davidson
V L
VL
Huizinga
E G
EG
Vellieux
F M
FM
Duine
J A
JA
Hol
W G
WG
D001665:Binding Sites; D006860:Hydrogen Bonding; D045563:Indolequinones; D046911:Macromolecular Substances; D008958:Models, Molecular; D015394:Molecular Structure; D010084:Oxidation-Reduction; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000737:chemistry*; D010231:Paracoccus denitrificans / Q000201:enzymology*; D011809:Quinones / Q000737:chemistry*; D013855:Thiobacillus / Q000201:enzymology*; D014364:Tryptophan / Q000031:analogs & derivatives* / Q000737:chemistry; D014961:X-Ray Diffraction
D045563:Indolequinones; D046911:Macromolecular Substances; D011809:Quinones; C070569:tryptophan tryptophylquinone; D014364:Tryptophan; C021567:methylamine dehydrogenase; D000587:Oxidoreductases Acting on CH-NH Group Donors