186 related articles for article (PubMed ID: 21128656)
1. The tightly bound calcium of MauG is required for tryptophan tryptophylquinone cofactor biosynthesis.
Shin S; Feng M; Chen Y; Jensen LM; Tachikawa H; Wilmot CM; Liu A; Davidson VL
Biochemistry; 2011 Jan; 50(1):144-50. PubMed ID: 21128656
[TBL] [Abstract][Full Text] [Related]
2. 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]
3. 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]
4. 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]
5. Proline 107 is a major determinant in maintaining the structure of the distal pocket and reactivity of the high-spin heme of MauG.
Feng M; Jensen LM; Yukl ET; Wei X; Liu A; Wilmot CM; Davidson VL
Biochemistry; 2012 Feb; 51(8):1598-606. PubMed ID: 22299652
[TBL] [Abstract][Full Text] [Related]
6. 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]
7. 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]
8. 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]
9. A Trp199Glu MauG variant reveals a role for Trp199 interactions with pre-methylamine dehydrogenase during tryptophan tryptophylquinone biosynthesis.
Abu Tarboush N; Jensen LM; Wilmot CM; Davidson VL
FEBS Lett; 2013 Jun; 587(12):1736-41. PubMed ID: 23669364
[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. Crystal structures of CO and NO adducts of MauG in complex with pre-methylamine dehydrogenase: implications for the mechanism of dioxygen activation.
Yukl ET; Goblirsch BR; Davidson VL; Wilmot CM
Biochemistry; 2011 Apr; 50(14):2931-8. PubMed ID: 21355604
[TBL] [Abstract][Full Text] [Related]
12. A T67A mutation in the proximal pocket of the high-spin heme of MauG stabilizes formation of a mixed-valent FeII/FeIII state and enhances charge resonance stabilization of the bis-FeIV state.
Shin S; Feng M; Li C; Williamson HR; Choi M; Wilmot CM; Davidson VL
Biochim Biophys Acta; 2015 Aug; 1847(8):709-16. PubMed ID: 25896561
[TBL] [Abstract][Full Text] [Related]
13. 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; 69(Pt 7):738-43. PubMed ID: 23832199
[TBL] [Abstract][Full Text] [Related]
14. 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]
15. 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]
16. 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]
17. 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]
18. Functional importance of tyrosine 294 and the catalytic selectivity for the bis-Fe(IV) state of MauG revealed by replacement of this axial heme ligand with histidine .
Abu Tarboush N; Jensen LM; Feng M; Tachikawa H; Wilmot CM; Davidson VL
Biochemistry; 2010 Nov; 49(45):9783-91. PubMed ID: 20929212
[TBL] [Abstract][Full Text] [Related]
19. 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]
20. Effects of the loss of the axial tyrosine ligand of the low-spin heme of MauG on its physical properties and reactivity.
Abu Tarboush N; Shin S; Geng J; Liu A; Davidson VL
FEBS Lett; 2012 Dec; 586(24):4339-43. PubMed ID: 23127557
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]