Premium
Crystallographic investigations of the tryptophan‐derived cofactor in the quinoprotein methylamine dehydrogenase
Author(s) -
Chen Longyin,
Mathews F.Scott,
Davidson Victor L.,
Huizinga Eric G.,
Vellieux Frederic M.D.,
Duine Johannis A.,
Hol Wim G.J.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80041-z
Subject(s) - cofactor , chemistry , methylamine , thiobacillus , dehydrogenase , carbon monoxide dehydrogenase , biochemistry , stereochemistry , enzyme , organic chemistry , sulfur , catalysis , carbon monoxide
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.