2019
DOI: 10.1002/chem.201904020
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Uno Ferro, a de novo Designed Protein, Binds Transition Metals with High Affinity and Stabilizes Semiquinone Radical Anion

Abstract: Metalloenzymes often utilize radicals in order to facilitate chemical reactions. Recently, DeGrado and co‐workers have discovered that model proteins can efficiently stabilize semiquinone radical anion produced by oxidation of 3,5‐di‐tert‐butylcatechol (DTBC) in the presence of two zinc ions. Here, we show that the number and the nature of metal ions have relatively minor effect on semiquinone stabilization in model proteins, with a single metal ion being sufficient for radical stabilization. The radical is st… Show more

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Cited by 9 publications
(3 citation statements)
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“…We next evaluated the ability of DFP3 to bind to and stabilize a reactive substrate at its dimetal active site. We previously demonstrated the redox-inert di-Zn 2+ form of a single-domain DF protein is capable of binding to and stabilizing the otherwise highly reactive radical semiquinone form of 3,5-di-tert-butylcatechol (DTBC) ( 58 , 59 ). In aqueous solution, the semiquinone form of DTBC is much less stable than either the corresponding catechol or quinone (DTBQ).…”
Section: Resultsmentioning
confidence: 99%
“…We next evaluated the ability of DFP3 to bind to and stabilize a reactive substrate at its dimetal active site. We previously demonstrated the redox-inert di-Zn 2+ form of a single-domain DF protein is capable of binding to and stabilizing the otherwise highly reactive radical semiquinone form of 3,5-di-tert-butylcatechol (DTBC) ( 58 , 59 ). In aqueous solution, the semiquinone form of DTBC is much less stable than either the corresponding catechol or quinone (DTBQ).…”
Section: Resultsmentioning
confidence: 99%
“…Therefore, the reversible transformation of phenol-SQ-quinone in PDA films under oxidative stress is closely related to changes in vascular wall cells and inflammatory cells. 14 Na 2 S 2 O 3 has been used as a stabilizer for studying SQ radicals in vitro [15][16][17] and oxidative stress can be simulated through ultraviolet (UV) irradiation of a hydrogen peroxide diluent. 18,19 Therefore, we studied the reversible transformation of phenol-SQ-quinone in PDA films using Na 2 S 2 O 3 to stabilize SQ, and using a hydrogen peroxide diluent and UV irradiation to simulate oxidative stress.…”
Section: Introductionmentioning
confidence: 99%
“…Compared to the titanium citrate controls, densitometric analysis showed that the Ti 4+ –DFsc complex depleted 80% of the supercoiled DNA signal over 24 h. In contrast, the apoprotein led to only 20% depletion of this signal over the same period. While the observed apoprotein activity may be due, in part, to protein alone, it could also be ascribed to metal contamination because trace concentrations of a broad range of metals have previously been identified in apo-DFsc samples and DNA cleavage experiments conducted in the presence of excess ethylenediaminetetraacetic acid resulted in a loss of activity (Figure S3). The total DNA signal intensity is decreased by an average of 40% in samples incubated with Ti 4+ –DFsc compared to DNA alone, apo-DFsc, and Ti 4+ alone treated samples because of further cleavage of form III to produce undetected forms of DNA.…”
mentioning
confidence: 99%