151 related articles for article (PubMed ID: 17073448)
1. Mechanistic possibilities in MauG-dependent tryptophan tryptophylquinone biosynthesis.
Li X; Jones LH; Pearson AR; Wilmot CM; Davidson VL
Biochemistry; 2006 Nov; 45(44):13276-83. PubMed ID: 17073448
[TBL] [Abstract][Full Text] [Related]
2. Further insights into quinone cofactor biogenesis: probing the role of mauG in methylamine dehydrogenase tryptophan tryptophylquinone formation.
Pearson AR; De La Mora-Rey T; Graichen ME; Wang Y; Jones LH; Marimanikkupam S; Agger SA; Grimsrud PA; Davidson VL; Wilmot CM
Biochemistry; 2004 May; 43(18):5494-502. PubMed ID: 15122915
[TBL] [Abstract][Full Text] [Related]
3. MauG-dependent in vitro biosynthesis of tryptophan tryptophylquinone in methylamine dehydrogenase.
Wang Y; Li X; Jones LH; Pearson AR; Wilmot CM; Davidson VL
J Am Chem Soc; 2005 Jun; 127(23):8258-9. PubMed ID: 15941239
[TBL] [Abstract][Full Text] [Related]
4. Kinetic mechanism for the initial steps in MauG-dependent tryptophan tryptophylquinone biosynthesis.
Lee S; Shin S; Li X; Davidson VL
Biochemistry; 2009 Mar; 48(11):2442-7. PubMed ID: 19196017
[TBL] [Abstract][Full Text] [Related]
5. Mutation of Trp(93) of MauG to tyrosine causes loss of bound Ca(2+) and alters the kinetic mechanism of tryptophan tryptophylquinone cofactor biosynthesis.
Shin S; Feng M; Davidson VL
Biochem J; 2013 Nov; 456(1):129-37. PubMed ID: 24024544
[TBL] [Abstract][Full Text] [Related]
6. Kinetic and physical evidence that the diheme enzyme MauG tightly binds to a biosynthetic precursor of methylamine dehydrogenase with incompletely formed tryptophan tryptophylquinone.
Li X; Fu R; Liu A; Davidson VL
Biochemistry; 2008 Mar; 47(9):2908-12. PubMed ID: 18220357
[TBL] [Abstract][Full Text] [Related]
7. Mutagenesis of tryptophan199 suggests that hopping is required for MauG-dependent tryptophan tryptophylquinone biosynthesis.
Tarboush NA; Jensen LM; Yukl ET; Geng J; Liu A; Wilmot CM; Davidson VL
Proc Natl Acad Sci U S A; 2011 Oct; 108(41):16956-61. PubMed ID: 21969534
[TBL] [Abstract][Full Text] [Related]
8. Long-range electron transfer reactions between hemes of MauG and different forms of tryptophan tryptophylquinone of methylamine dehydrogenase.
Shin S; Abu Tarboush N; Davidson VL
Biochemistry; 2010 Jul; 49(27):5810-6. PubMed ID: 20540536
[TBL] [Abstract][Full Text] [Related]
9. Posttranslational biosynthesis of the protein-derived cofactor tryptophan tryptophylquinone.
Davidson VL; Wilmot CM
Annu Rev Biochem; 2013; 82():531-50. PubMed ID: 23746262
[TBL] [Abstract][Full Text] [Related]
10. Tryptophan tryptophylquinone biosynthesis: a radical approach to posttranslational modification.
Davidson VL; Liu A
Biochim Biophys Acta; 2012 Nov; 1824(11):1299-305. PubMed ID: 22314272
[TBL] [Abstract][Full Text] [Related]
11. Carboxyl group of Glu113 is required for stabilization of the diferrous and bis-Fe(IV) states of MauG.
Abu Tarboush N; Yukl ET; Shin S; Feng M; Wilmot CM; Davidson VL
Biochemistry; 2013 Sep; 52(37):6358-67. PubMed ID: 23952537
[TBL] [Abstract][Full Text] [Related]
12. MauG, a novel diheme protein required for tryptophan tryptophylquinone biogenesis.
Wang Y; Graichen ME; Liu A; Pearson AR; Wilmot CM; Davidson VL
Biochemistry; 2003 Jun; 42(24):7318-25. PubMed ID: 12809487
[TBL] [Abstract][Full Text] [Related]
13. Evidence for redox cooperativity between c-type hemes of MauG which is likely coupled to oxygen activation during tryptophan tryptophylquinone biosynthesis.
Li X; Feng M; Wang Y; Tachikawa H; Davidson VL
Biochemistry; 2006 Jan; 45(3):821-8. PubMed ID: 16411758
[TBL] [Abstract][Full Text] [Related]
14. Isotope labeling studies reveal the order of oxygen incorporation into the tryptophan tryptophylquinone cofactor of methylamine dehydrogenase.
Pearson AR; Marimanikkuppam S; Li X; Davidson VL; Wilmot CM
J Am Chem Soc; 2006 Sep; 128(38):12416-7. PubMed ID: 16984182
[TBL] [Abstract][Full Text] [Related]
15. In crystallo posttranslational modification within a MauG/pre-methylamine dehydrogenase complex.
Jensen LM; Sanishvili R; Davidson VL; Wilmot CM
Science; 2010 Mar; 327(5971):1392-4. PubMed ID: 20223990
[TBL] [Abstract][Full Text] [Related]
16. MauG, a diheme enzyme that catalyzes tryptophan tryptophylquinone biosynthesis by remote catalysis.
Shin S; Davidson VL
Arch Biochem Biophys; 2014 Feb; 544():112-8. PubMed ID: 24144526
[TBL] [Abstract][Full Text] [Related]
17. Suicide inactivation of MauG during reaction with O(2) or H(2)O(2) in the absence of its natural protein substrate.
Shin S; Lee S; Davidson VL
Biochemistry; 2009 Oct; 48(42):10106-12. PubMed ID: 19788236
[TBL] [Abstract][Full Text] [Related]
18. Electron transfer from the aminosemiquinone reaction intermediate of methylamine dehydrogenase to amicyanin.
Bishop GR; Davidson VL
Biochemistry; 1998 Aug; 37(31):11026-32. PubMed ID: 9692997
[TBL] [Abstract][Full Text] [Related]
19. MauG: a di-heme enzyme required for methylamine dehydrogenase maturation.
Wilmot CM; Yukl ET
Dalton Trans; 2013 Mar; 42(9):3127-35. PubMed ID: 23086017
[TBL] [Abstract][Full Text] [Related]
20. 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; 35(27):8948-54. PubMed ID: 8688431
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
