J
Jack E. Baldwin
Researcher at University of Oxford
Publications - 636
Citations - 15177
Jack E. Baldwin is an academic researcher from University of Oxford. The author has contributed to research in topics: Isopenicillin N synthase & Amino acid. The author has an hindex of 56, co-authored 636 publications receiving 14749 citations. Previous affiliations of Jack E. Baldwin include Ghent University & G. D. Searle & Company.
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Journal ArticleDOI
Crystal structure of isopenicillin N synthase is the first from a new structural family of enzymes
Peter L. Roach,Ian J. Clifton,Vilmos Fülöp,Karl Harlos,Geoffrey J. Barton,Janos Hajdu,Inger Andersson,Inger Andersson,Christopher J. Schofield,Jack E. Baldwin +9 more
TL;DR: The structure of isopenicillin N synthase (IPNS) complexed with manganese was reported in this paper, which reveals the active site is unusually buried within a "jelly-roll" motif and lined by hydrophobic residues.
Journal ArticleDOI
Structure of isopenicillin N synthase complexed with substrate and the mechanism of penicillin formation.
Peter L. Roach,Ian J. Clifton,Charles M. H. Hensgens,Norio Shibata,Christopher J. Schofield,Janos Hajdu,Jack E. Baldwin +6 more
TL;DR: The crystal structure of IPNS complexed to ferrous iron and ACV, determined to 1.3 å resolution, suggests a mechanism for penicillin formation that involves ligation of ACV to the iron centre, creating a vacant iron coordination site into which dioxygen can bind.
Journal ArticleDOI
5-Endo-trigonal reactions: a disfavoured ring closure
Jack E. Baldwin,John Cutting,William A. Dupont,Lawrence Ivan Kruse,Lee Silberman,Richard C. Thomas +5 more
TL;DR: A number of polyfunctional molecules have been examined as substrates for the 5-Endo-Trigonal ring-forming reaction, and it has been found that for first-row elements this is a disfavoured process, alternative reactions of type 5-Exo-trig generally taking precedence.
Journal ArticleDOI
Structure of a cephalosporin synthase
Karin Valegård,Anke C. Terwisscha van Scheltinga,Matthew D. Lloyd,Takane Hara,S. Ramaswamy,Anastassis Perrakis,Andrew Thompson,H.J. Lee,Jack E. Baldwin,Christopher J. Schofield,Janos Hajdu,Inger Andersson +11 more
TL;DR: The first crystal structure of a 2-oxoacid-dependent oxygenase is reported, obtained from merohedrally twinned crystals, and a model based on these structures is proposed for ferryl formation, which is common to many mononuclear ferrous enzymes.