Biosynthesis of the pigments of life: mechanistic studies on the conversion of porphobilinogen to uroporphyrinogen III

Recent Progress in Porphyrin and Chlorophyll Biosynthesis

“…The porphyrins detected arose by oxidation of the corresponding porphyrinogen (hexahydroporphyrin) intermediates. This result with porphyric urines was confirmed more recently but the porphyrins from noimal urines suggest a random pattern of decarboxylation ( 15 1,152). Random patterns of decarboxylation were also observed when erythrocyte lysates were offered uro'gen I11 but the clockwise decarboxylation pattern was observed with PBG as substrate (152).…”

“…Literature studies (1,16,(131)(132)(133)(134)(135)(136)(137)(138)(139)(140)(141)(142)(143) show that this section of tetrapyrrole biosynthesis has been studied extensively in the laboratories of both Battersby and Jordan: only salient features of this reaction sequence are presented.…”

“…In the enzymic cyclization of hydroxymethylbilane I, ring D undergoes inversion around C-16 of hydroxymethylbilane I, which becomes the spiro carbon of a spiro intermediate, possibly a spirocyclic pyrrolenine (see Scheme 2) (1,147).…”

Syntheses of Calix[4]Pyrroles by Amberlyst-15 Catalyzed Cyclocondensations of Pyrrole with Selected Ketones

“…They find interesting applications as raw materials for transformation into novel calix [4]pyridines and calix [4]pyridinopyrroles [14], as new solid supports capable of separating anion mixtures [15], in optical recognition of organic vapors [16] and as biologically active species [17]. Porphyrinogens, bearing hydrogen atoms at meso positions, are key intermediates in biological and chemical synthesis of porphyrins [18,19]. Various attempts have been made for the development of milder methods for the synthesis of porphyrins [20][21][22], N-C isomerization [23,24] and higher homologues of porphyrins [25].…”

Accurate and highly complete synchrotron protein crystal Laue diffraction data using the ESRF CCD and the Daresbury Laue software

“…As will be seen, accurate highly redundant and highly complete Laue diffraction data have been collected for a crystal of wild-type hydroxymethylbilane synthase (HMBS) from E. coli (crystal size $50 Â 500 Â 500 mm 3 ), for which re®ned coordinates and structure factors have been deposited with the PDB (access codes 2YPN and 2YPNSF). HMBS (EC 4.3.1.8) catalyses the conversion of porphobilinogen to hydroxymethylbilane, an intermediate in the biosynthesis of tetrapyrrolic pigments such as haem, chlorophyll and vitamin B12 (Battersby & Leeper, 1990).…”