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5. Structure, function, and applications of tryptophan tryptophylquinone enzymes. Davidson VL. Adv Exp Med Biol; 1999; 467():587-95. PubMed ID: 10721104 [Abstract] [Full Text] [Related]
6. Intermolecular electron transfer from substrate-reduced methylamine dehydrogenase to amicyanin is linked to proton transfer. Bishop GR, Davidson VL. Biochemistry; 1995 Sep 19; 34(37):12082-6. PubMed ID: 7547947 [Abstract] [Full Text] [Related]
7. Aromatic amine dehydrogenase, a second tryptophan tryptophylquinone enzyme. Govindaraj S, Eisenstein E, Jones LH, Sanders-Loehr J, Chistoserdov AY, Davidson VL, Edwards SL. J Bacteriol; 1994 May 19; 176(10):2922-9. PubMed ID: 8188594 [Abstract] [Full Text] [Related]
8. Evidence for a tryptophan tryptophylquinone aminosemiquinone intermediate in the physiologic reaction between methylamine dehydrogenase and amicyanin. Bishop GR, Brooks HB, Davidson VL. Biochemistry; 1996 Jul 09; 35(27):8948-54. PubMed ID: 8688431 [Abstract] [Full Text] [Related]
9. Active-site residues are critical for the folding and stability of methylamine dehydrogenase. Sun D, Jones LH, Mathews FS, Davidson VL. Protein Eng; 2001 Sep 09; 14(9):675-81. PubMed ID: 11707614 [Abstract] [Full Text] [Related]
10. Crystallographic investigations of the tryptophan-derived cofactor in the quinoprotein methylamine dehydrogenase. Chen LY, Mathews FS, Davidson VL, Huizinga EG, Vellieux FM, Duine JA, Hol WG. FEBS Lett; 1991 Aug 05; 287(1-2):163-6. PubMed ID: 1879526 [Abstract] [Full Text] [Related]
11. Spectroscopic evidence for a common electron transfer pathway for two tryptophan tryptophylquinone enzymes. Edwards SL, Davidson VL, Hyun YL, Wingfield PT. J Biol Chem; 1995 Mar 03; 270(9):4293-8. PubMed ID: 7876189 [Abstract] [Full Text] [Related]
12. Structures of MauG in complex with quinol and quinone MADH. Yukl ET, Jensen LM, Davidson VL, Wilmot CM. Acta Crystallogr Sect F Struct Biol Cryst Commun; 2013 Jul 03; 69(Pt 7):738-43. PubMed ID: 23832199 [Abstract] [Full Text] [Related]
13. Catalysis by the isolated tryptophan tryptophylquinone-containing subunit of aromatic amine dehydrogenase is distinct from native enzyme and synthetic model compounds and allows further probing of TTQ mechanism. Hothi P, Lee M, Cullis PM, Leys D, Scrutton NS. Biochemistry; 2008 Jan 08; 47(1):183-94. PubMed ID: 18052255 [Abstract] [Full Text] [Related]
17. Posttranslational biosynthesis of the protein-derived cofactor tryptophan tryptophylquinone. Davidson VL, Wilmot CM. Annu Rev Biochem; 2013 Jan 08; 82():531-50. PubMed ID: 23746262 [Abstract] [Full Text] [Related]
18. Electrostatic environment of the tryptophylquinone cofactor in methylamine dehydrogenase: evidence from resonance Raman spectroscopy of model compounds. Moënne-Loccoz P, Nakamura N, Itoh S, Fukuzumi S, Gorren AC, Duine JA, Sanders-Loehr J. Biochemistry; 1996 Apr 16; 35(15):4713-20. PubMed ID: 8664261 [Abstract] [Full Text] [Related]
19. Catalytic role of monovalent cations in the mechanism of proton transfer which gates an interprotein electron transfer reaction. Bishop GR, Davidson VL. Biochemistry; 1997 Nov 04; 36(44):13586-92. PubMed ID: 9354627 [Abstract] [Full Text] [Related]
20. Tryptophan tryptophylquinone cofactor biogenesis in the aromatic amine dehydrogenase of Alcaligenes faecalis. Cofactor assembly and catalytic properties of recombinant enzyme expressed in Paracoccus denitrificans. Hothi P, Khadra KA, Combe JP, Leys D, Scrutton NS. FEBS J; 2005 Nov 04; 272(22):5894-909. PubMed ID: 16279953 [Abstract] [Full Text] [Related] Page: [Next] [New Search]