Walsh CT - Search Results

1

Purification, crystallization, and preliminary x-ray diffraction studies of the flavoenzyme mercuric ion reductase from Bacillus sp. strain RC607.

Moore MJ, Distefano MD, Walsh CT, Schiering N, Pai EF. Moore MJ, et al. Among authors: walsh ct. J Biol Chem. 1989 Aug 25;264(24):14386-8. J Biol Chem. 1989. PMID: 2668287 Free article.

2

Active site of mercuric reductase resides at the subunit interface and requires Cys135 and Cys140 from one subunit and Cys558 and Cys559 from the adjacent subunit: evidence from in vivo and in vitro heterodimer formation.

Distefano MD, Moore MJ, Walsh CT. Distefano MD, et al. Among authors: walsh ct. Biochemistry. 1990 Mar 20;29(11):2703-13. doi: 10.1021/bi00463a013. Biochemistry. 1990. PMID: 2189495

3

Mutagenesis of the N- and C-terminal cysteine pairs of Tn501 mercuric ion reductase: consequences for bacterial detoxification of mercurials.

Moore MJ, Walsh CT. Moore MJ, et al. Among authors: walsh ct. Biochemistry. 1989 Feb 7;28(3):1183-94. doi: 10.1021/bi00429a036. Biochemistry. 1989. PMID: 2540817

4

Mutagenesis of the redox-active disulfide in mercuric ion reductase: catalysis by mutant enzymes restricted to flavin redox chemistry.

Distefano MD, Au KG, Walsh CT. Distefano MD, et al. Among authors: walsh ct. Biochemistry. 1989 Feb 7;28(3):1168-83. doi: 10.1021/bi00429a035. Biochemistry. 1989. PMID: 2653436

5

X-ray crystallographic studies of the alanine-specific racemase from Bacillus stearothermophilus. Overproduction, crystallization, and preliminary characterization.

Neidhart DJ, Distefano MD, Tanizawa K, Soda K, Walsh CT, Petsko GA. Neidhart DJ, et al. Among authors: walsh ct. J Biol Chem. 1987 Nov 15;262(32):15323-6. J Biol Chem. 1987. PMID: 3680197 Free article.

6

C-terminal cysteines of Tn501 mercuric ion reductase.

Moore MJ, Miller SM, Walsh CT. Moore MJ, et al. Among authors: walsh ct. Biochemistry. 1992 Feb 18;31(6):1677-85. doi: 10.1021/bi00121a015. Biochemistry. 1992. PMID: 1531297

7

Use of a site-directed triple mutant to trap intermediates: demonstration that the flavin C(4a)-thiol adduct and reduced flavin are kinetically competent intermediates in mercuric ion reductase.

Miller SM, Massey V, Ballou D, Williams CH Jr, Distefano MD, Moore MJ, Walsh CT. Miller SM, et al. Among authors: walsh ct. Biochemistry. 1990 Mar 20;29(11):2831-41. doi: 10.1021/bi00463a028. Biochemistry. 1990. PMID: 2189497

8

Evidence for the participation of Cys558 and Cys559 at the active site of mercuric reductase.

Miller SM, Moore MJ, Massey V, Williams CH Jr, Distefano MD, Ballou DP, Walsh CT. Miller SM, et al. Among authors: walsh ct. Biochemistry. 1989 Feb 7;28(3):1194-205. doi: 10.1021/bi00429a037. Biochemistry. 1989. PMID: 2653437

9

Molecular basis of bacterial resistance to organomercurial and inorganic mercuric salts.

Walsh CT, Distefano MD, Moore MJ, Shewchuk LM, Verdine GL. Walsh CT, et al. FASEB J. 1988 Feb;2(2):124-30. doi: 10.1096/fasebj.2.2.3277886. FASEB J. 1988. PMID: 3277886 Review.

10

Structure of the detoxification catalyst mercuric ion reductase from Bacillus sp. strain RC607.

Schiering N, Kabsch W, Moore MJ, Distefano MD, Walsh CT, Pai EF. Schiering N, et al. Among authors: walsh ct. Nature. 1991 Jul 11;352(6331):168-72. doi: 10.1038/352168a0. Nature. 1991. PMID: 2067577

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