Preaching to Princes: John Burgess and George Hakewill in the Royal Pulpit

This article examines a previously unnoticed link between the Puritan John Burgess and the Calvinist conformist George Hakewill. In 1604 Burgess preached a court sermon so outspoken and critical of James I’s religious policy that he was imprisoned. Nearly twenty years later, however, Hakewill chose to incorporate extended passages from Burgess’s sermon into the series of sermons, King David’s vow (1621), preached to Prince Charles’s household. This article considers why Burgess’s sermon became so resonant for Hakewill in the early 1620s and also demonstrates how Hakewill deliberately sought to moderate Burgess’s strident polemic. In so doing the article provides important new evidence for the politically attuned sermon culture at Prince Charles’s court in the early 1620s and also suggests how, as the parameters for clerical conformity shifted in the latter years of James’s reign, Calvinist conformists found a new appeal in the works of moderate Puritans. I

"Producers and Consumers in EU E-Commerce Law by John Dickie, Oxford: Hart Publishing, 2005 (ISBN 1-841-13454-6)"

Book Review

John P. Mackintosh, Devolution and the Union

This article provides a discussion of the political thinking of John P. Mackintosh (1929–1978) around the debate over Scottish devolution, and the constitutional reform of the UK, during the 1960s and 1970s. The article explores Mackintosh's ‘Union State’ vision of the UK and connects this to his interest in, and study of, the Northern Ireland experience of devolution from 1921 to 1972. It also considers the significance of Mackintosh's confrontations with Scottish nationalism and suggests that his unionism was representative of a more authentic and rooted tradition than is usually acknowledged. The article offers an evaluation of Mackintosh's legacy and considers the extent to which the questions he posed, and the lines of argument he advanced, have retained their relevance and interest in the new context of partial devolution in the UK, and in the current period of renewed constitutional speculation and debate over the future of the Union and the UK.

Epistolarum Familiarium Liber Unus in The Complete Works of John Milton: Volume XI (672pp.)

This edition of Milton’s Epistolarum Familiarium Liber Unus and of his Uncollected Letters, will appear as 672 pp. of The Complete Works of John Milton Volume XI, eds. Gordon Campbell and Edward Jones (Oxford University Press, forthcoming 2016). A diplomatic Latin text and a new facing English translation are complemented by a detailed Introduction and commentary that situate Milton’s Latin letters in relation to the classical, pedagogical and essentially humanist contexts at the heart of their composition. Now the art of epistolography advocated and exemplified by Cicero and Quintilian and embraced by Renaissance pedagogical manuals is read through a humanist filter whereby, via the precedent (and very title) of Epistolae Familiares, the Miltonic Liber is shown to engage with a neo-Latin re-invention of the classical epistola that had come to birth in quattrocento Italy in the letters of Petrarch and his contemporaries. At the same time the Epistolae are seen as offering fresh insight into Milton’s views on education, philology, his relations with Italian literati, his blindness, the poetic dimension of his Latin prose, and especially his verbal ingenuity as the ‘words’ of Latin ‘Letters’ become a self-conscious showcasing of etymological punning on the ‘letters’ of Latin ‘words’. The edition also announces several new discoveries, most notably its uncovering and collation of a manuscript of Henry Oldenburg’s transcription (in his Liber Epistolaris held in Royal Society, London) of Milton’s Ep. Fam. 25 (to Richard Jones). Oldenburg’s transcription (from the original sent to his pupil Jones) is an important find, given the loss of all but two of the manuscripts of Milton’s original Latin letters included in the 1674 volume. The edition also presents new evidence in regard to Milton’s relationships with the Italian philologist Benedetto Buonmattei, the Greek humanist Leonard Philaras, the radical pastor Jean Labadie (and the French church of London), and the elusive Peter Heimbach.

Divergence of chemical function in the alkaline phosphatase superfamily: Structure and mechanism of the P-C bond cleaving enzyme phosphonoacetate hydrolase

Phosphonates constitute a class of natural products that mimic the properties of the more common organophosphate ester metabolite yet are not readily degraded owing to the direct linkage of the phosphorus atom to the carbon atom. Phosphonate hydrolases have evolved to allow bacteria to utilize environmental phosphonates as a source of carbon and phosphorus. The work reported in this paper examines one such enzyme, phosphonoacetate hydrolase. By using a bioinformatic approach, we circumscribed the biological range of phosphonoacetate hydrolase to a select group of bacterial species from different classes of Proteobacteria. In addition, using gene context, we identified a novel 2-aminoethylphosphonate degradation pathway in which phosphonoacetate hydrolase is a participant. The X-ray structure of phosphonoformate-bound phosphonoacetate hydrolase was determined to reveal that this enzyme is most closely related to nucleotide pyrophosphatase/diesterase, a promiscuous two-zinc ion metalloenzyme of the alkaline phosphatase enzyme superfamily. The X-ray structure and metal ion specificity tests showed that phosphonoacetate hydrolase is also a two-zinc ion metalloenzyme. By using site-directed mutagenesis and P-32-labeling strategies, the catalytic nucleophile was shown to be Thr64. A structure-guided, site-directed mutation-based inquiry of the catalytic contributions of active site residues identified Lys126 and Lys128 as the most likely candidates for stabilization of the aci-carboxylate dianion leaving group. A catalytic mechanism is proposed which combines Lys12/Lys128 leaving group stabilization with zinc ion activation of the Thr64 nucleophile and the substrate phosphoryl group.