Author
Andrew R. Hyde
Bio: Andrew R. Hyde is an academic researcher from University of St Andrews. The author has contributed to research in topics: Carbon-13 NMR & Ion. The author has an hindex of 6, co-authored 12 publications receiving 180 citations.
Papers
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TL;DR: In this paper, the diamagnetic Roussin esters Fe 2 (SR) 2 (NO) 4 readily underwent exchange with thiols R′SH to yield Fe 2(SR′) 2(NO)4 : the exchange was faster in polar, coordinating solvents where paramagnetic, mononuclear complexes of types [Fe(NO)-2 (solvent) 2 ] + and Fe(NO)(solvent), were formed.
57 citations
48 citations
TL;DR: In this article, the activation parameters for the C2h⇌C2v reaction are reported and two isomers in solution are assumed to have structures of C 2h and C 2v, symmetry.
30 citations
20 citations
TL;DR: In this paper, it was shown that the 15 N N NMR spectrum of [Fe 4 Se 3 (15 NO) 7 ] provides a definitive proof of the structure for this anion.
8 citations
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1,133 citations
TL;DR: In this article, it was shown that low (nanomolar) concentrations of NO specifically inhibit cytochrome oxidase in competition with oxygen, and this inhibition is fully reversible when NO is removed.
698 citations
320 citations
TL;DR: The radical nature of NO cannot account for its cytotoxicity, but its reaction with superoxide to form peroxynitite and highly reactive hydroxyl radicals may be important in this context.
316 citations
TL;DR: It is shown here that SoxR activation by NO occurs through direct modification of the [2Fe-2S] centers to form protein-bound dinitrosyl-iron-dithiol adducts, which is observed both in intact bacterial cells and in purified SoxR after NO treatment.
Abstract: Nitric oxide (NO) has diverse roles in intercellular communication and (at higher levels) in immune-mediated cell killing. NO reacts with many cellular targets, with cell-killing effects correlated to inactivation of key enzymes through nitrosylation of their iron-sulfur centers. SoxR protein, a redox-sensitive transcription activator dependent on the oxidation state of its binuclear iron-sulfur ([2Fe-2S]) centers, is also activated in Escherichia coli on exposure to macrophage-generated NO. We show here that SoxR activation by NO occurs through direct modification of the [2Fe-2S] centers to form protein-bound dinitrosyl-iron-dithiol adducts, which we have observed both in intact bacterial cells and in purified SoxR after NO treatment. Functional activation through nitrosylation of iron-sulfur centers contrasts with the inactivation typically caused by this modification. Purified, nitrosylated SoxR has transcriptional activity similar to that of oxidized SoxR and is relatively stable. In contrast, nitrosylated SoxR is short-lived in intact cells, indicative of mechanisms that actively dispose of nitrosylated iron-sulfur centers.
298 citations