Some comparisons between solution and crystal properties of thiosulfate sulfurtransferase

Paul M. Horowitz; Kuldeep Patel

doi:10.1016/0006-291X(80)91247-4

Some comparisons between solution and crystal properties of thiosulfate sulfurtransferase

Paul M. Horowitz, Kuldeep Patel

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Abstract

The activity and crystal stability of the enzyme thiosulfate sulfurtransferase were studied as a function of ionic strength. At 2 M ammonium sulfate, where the x-ray structural studies of this protein were done soluble enzyme has low activity (<16% of the activity of the enzyme at an ionic strength of 0.1) and crystals of the enzyme are stable when substrates are added. However, at 1.4 M ammonium sulfate, crystals of TST rapidly dissolve in 1 mM CN^- but are relatively stable in 1 mM S₂O₃⁼. These results are consistent with a conformational change on converting the sulfur substituted form of the enzyme (ES) to the sulfur-free form (E) and helps to explain why this change was not observed in the crystallographic studies.

Original language	English (US)
Pages (from-to)	419-423
Number of pages	5
Journal	Biochemical and Biophysical Research Communications
Volume	94
Issue number	2
DOIs	https://doi.org/10.1016/0006-291X(80)91247-4
State	Published - May 30 1980
Externally published	Yes

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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abstract = "The activity and crystal stability of the enzyme thiosulfate sulfurtransferase were studied as a function of ionic strength. At 2 M ammonium sulfate, where the x-ray structural studies of this protein were done soluble enzyme has low activity (<16% of the activity of the enzyme at an ionic strength of 0.1) and crystals of the enzyme are stable when substrates are added. However, at 1.4 M ammonium sulfate, crystals of TST rapidly dissolve in 1 mM CN- but are relatively stable in 1 mM S2O3=. These results are consistent with a conformational change on converting the sulfur substituted form of the enzyme (ES) to the sulfur-free form (E) and helps to explain why this change was not observed in the crystallographic studies.",

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AU - Horowitz, Paul M.

AU - Patel, Kuldeep

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N2 - The activity and crystal stability of the enzyme thiosulfate sulfurtransferase were studied as a function of ionic strength. At 2 M ammonium sulfate, where the x-ray structural studies of this protein were done soluble enzyme has low activity (<16% of the activity of the enzyme at an ionic strength of 0.1) and crystals of the enzyme are stable when substrates are added. However, at 1.4 M ammonium sulfate, crystals of TST rapidly dissolve in 1 mM CN- but are relatively stable in 1 mM S2O3=. These results are consistent with a conformational change on converting the sulfur substituted form of the enzyme (ES) to the sulfur-free form (E) and helps to explain why this change was not observed in the crystallographic studies.

AB - The activity and crystal stability of the enzyme thiosulfate sulfurtransferase were studied as a function of ionic strength. At 2 M ammonium sulfate, where the x-ray structural studies of this protein were done soluble enzyme has low activity (<16% of the activity of the enzyme at an ionic strength of 0.1) and crystals of the enzyme are stable when substrates are added. However, at 1.4 M ammonium sulfate, crystals of TST rapidly dissolve in 1 mM CN- but are relatively stable in 1 mM S2O3=. These results are consistent with a conformational change on converting the sulfur substituted form of the enzyme (ES) to the sulfur-free form (E) and helps to explain why this change was not observed in the crystallographic studies.

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Some comparisons between solution and crystal properties of thiosulfate sulfurtransferase

Abstract

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