Davidson VL - Search Results

1

Protein-derived cofactors. Expanding the scope of post-translational modifications.

Davidson VL. Davidson VL. Biochemistry. 2007 May 8;46(18):5283-92. doi: 10.1021/bi700468t. Epub 2007 Apr 17. Biochemistry. 2007. PMID: 17439161 Review.

2

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. Shin S, et al. Among authors: davidson vl. Biochemistry. 2010 Jul 13;49(27):5810-6. doi: 10.1021/bi1004969. Biochemistry. 2010. PMID: 20540536 Free PMC article.

3

Generation of protein-derived redox cofactors by posttranslational modification.

Davidson VL. Davidson VL. Mol Biosyst. 2011 Jan;7(1):29-37. doi: 10.1039/c005311b. Epub 2010 Oct 8. Mol Biosyst. 2011. PMID: 20936199 Review.

4

MauG, a novel diheme protein required for tryptophan tryptophylquinone biogenesis.

Wang Y, Graichen ME, Liu A, Pearson AR, Wilmot CM, Davidson VL. Wang Y, et al. Among authors: davidson vl. Biochemistry. 2003 Jun 24;42(24):7318-25. doi: 10.1021/bi034243q. Biochemistry. 2003. PMID: 12809487

5

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. Shin S, et al. Among authors: davidson vl. Biochemistry. 2009 Oct 27;48(42):10106-12. doi: 10.1021/bi901284e. Biochemistry. 2009. PMID: 19788236 Free PMC article.

6

pH-dependent semiquinone formation by methylamine dehydrogenase from Paracoccus denitrificans. Evidence for intermolecular electron transfer between quinone cofactors.

Davidson VL, Jones LH, Kumar MA. Davidson VL, et al. Biochemistry. 1990 Dec 4;29(48):10786-91. doi: 10.1021/bi00500a010. Biochemistry. 1990. PMID: 2271681

7

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. Li X, et al. Among authors: davidson vl. Biochemistry. 2006 Jan 24;45(3):821-8. doi: 10.1021/bi052000n. Biochemistry. 2006. PMID: 16411758 Free PMC article.

8

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. Li X, et al. Among authors: davidson vl. Biochemistry. 2008 Mar 4;47(9):2908-12. doi: 10.1021/bi702259w. Epub 2008 Jan 26. Biochemistry. 2008. PMID: 18220357

9

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. Abu Tarboush N, et al. Among authors: davidson vl. Biochemistry. 2010 Nov 16;49(45):9783-91. doi: 10.1021/bi101254p. Epub 2010 Oct 20. Biochemistry. 2010. PMID: 20929212 Free PMC article.

10

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. Feng M, et al. Among authors: davidson vl. Biochemistry. 2012 Feb 28;51(8):1598-606. doi: 10.1021/bi201882e. Epub 2012 Feb 10. Biochemistry. 2012. PMID: 22299652 Free PMC article.

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