Crystalline Rhodanese. I. Purification and Physicochemical Examination.

Sörbo, Bo; Lagerkvist, Ulf; Pesola, Rainer; Virtanen, Artturi I.; Sørensen, Nils Andreas

doi:10.3891/acta.chem.scand.07-1129

Cited by 321 publications

(106 citation statements)

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“…To study cellular modifications of the RhdA thiol we therefore used the thiosulfate:cyanide sulfurtransferase activity (TST, thiocyanate production) as a probe (Sörbo, 1953), for which the availability of the RhdA Cys 230 thiol is mandatory. As expected, considering the level of rhdA transcript and RhdA expression when gluconate was the carbon source (see Figures 3 and 5), TST activity was higher in extracts from gluconate-growths than in those from sucrose-growths ( Figure 6A; white bars).…”

Section: Outlining Redox-switch Modulation Of Rhdamentioning

confidence: 99%

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The rhodanese RhdA helps Azotobacter vinelandii in maintaining cellular redox balance

Remelli

Cereda

Papenbrock

et al. 2010

Biological Chemistry

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The tandem domain rhodanese-homology protein RhdA of Azotobacter vinelandii shows an active-site loop structure that confers structural peculiarity in the environment of its catalytic cysteine residue. The in vivo effects of the lack of RhdA were investigated using an A. vinelandii mutant strain (MV474) in which the rhdA gene was disrupted by deletion. Here, by combining analytical measurements and transcript profiles, we show that deletion of the rhdA gene generates an oxidative stress condition to which A. vinelandii responds by activating defensive mechanisms. In conditions of growth in the presence of the superoxide generator phenazine methosulfate, a stressor-dependent induction of rhdA gene expression was observed, thus highlighting that RhdA is important for A. vinelandii to sustain oxidative stress. The potential of RhdA to buffer general levels of oxidants in A. vinelandii cells via redox reactions involving its cysteine thiol is discussed.

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Section: Outlining Redox-switch Modulation Of Rhdamentioning

confidence: 99%

“…Thiosulfate:cyanide sulfurtransferase (TST) activity was tested by the discontinuous method described by Sörbo (1953 Chelatable iron (free iron) was determined according to Tangeras (1986). Cell-free extracts (approx.…”

Section: Analytical Proceduresmentioning

confidence: 99%

The rhodanese RhdA helps Azotobacter vinelandii in maintaining cellular redox balance

Remelli

Cereda

Papenbrock

et al. 2010

Biological Chemistry

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“…Denatured rhodanese was diluted 25-fold into the dilution buffer and pre-incubated at 30°C containing 50 mM potassium phosphate (pH 7.8), 50 mM Na&O,, 5 mM dithiothreitol, and indicated component(s). After incubation at 30°C for 30 min or indicated periods, reactivated rhodanese activity was determined according to Siirbo [17].…”

Section: Proteinsmentioning

confidence: 99%

Truncated GroEL monomer has the ability to promote folding of rhodanese without GroES and ATP

1993

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Similar to chaperonins from other sources, intact chaperonin from Escherichia coli (GroEL) exists as a tetradecamer, and the ability to promote folding of other proteins has been considered to be dependent on this oligomeric structure. However, the peptide fragments of GroEL of molecular size 34-50 kDa, which are produced by limited proteolysis of monomeric GroEL and are unable to assemble into an oligomer, retain the ability to promote folding of rhodanese even though the yield of productive folding is lower than the intact GroEL/GroES/ATP system. This promotion by truncated GroEL obeys rapid kinetics and does not require GroES and ATP.

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“…Other chemicals used were reagent grade and used without further purification. Crystalline rhodanese from beef kidney was prepared as previously described [15] and its activity was determined according to Sorbo [16]. Sulfur-free enzyme was obtained by adding 10 molar excess of cyanide to 1 ml of crystalline rhodanese dissolved in 50 mM sodium acetate.…”

Section: Methodsmentioning

confidence: 99%

Inactivation of Rhodanese by Pyridoxal 5′‐Phosphate

Cannella

Pecci

Costa

et al. 1975

European Journal of Biochemistry

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Pyridoxal 5'-phosphate and other aromatic aldehydes inactivate rhodanese. This inactivation reaches higher extents if the enzyme is in the sulfur-free form. The identification of the reactive residue as an amino group has been made by spectrophotometric determination of the 5'-phosphorylated pyridoxyl derivative of the enzyme. The inactivation increases with pyridoxal 5'-phosphate concentration and can be partially removed by adding thiosulfate or valine. Prolonged dialysis against phosphate buffer also leads to the enzyme reactivation. The absorption spectra of the pyridoxal phosphate-rhodanese complex show a peak at 410 nm related to the Schiff base and a shoulder in the 330nm region which is probably due to the reaction between pyridoxal 5'-phosphate and both the amino and thiol groups of the enzyme that appear reasonably close to each other. The relationship between loss of activity and pyridoxal 5'-phosphate binding to the enzyme shows that complete inactivation pyridoxal 5'-phosphate.

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Crystalline Rhodanese. I. Purification and Physicochemical Examination.

Cited by 321 publications

References 0 publications

The rhodanese RhdA helps Azotobacter vinelandii in maintaining cellular redox balance

The rhodanese RhdA helps Azotobacter vinelandii in maintaining cellular redox balance

Truncated GroEL monomer has the ability to promote folding of rhodanese without GroES and ATP

Inactivation of Rhodanese by Pyridoxal 5′‐Phosphate

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