Anaesthesia for caesarean section — a German survey

Stamer, Ulrike; Messerschmidt, Antje; Wulf, Hinnerk

doi:10.1111/j.1399-6576.1998.tb05301.x

Cited by 27 publications

(1 citation statement)

References 29 publications

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“…seems to rely more on an evolutionary relationo ft he (apo-)enzymes rathert han on simple cofactore xchange. [18] Boron is at race element relativelyu nexplored within the biological systemsc ontext. Despite its role in stabilizing plant cell walls via biopolymer cross-linking, borate-related compounds are knownt od isplay potenta ntibacterial activity (e.g.…”

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Reconstitution of Vanadium Haloperoxidase's Catalytic Activity by Boric Acid—Towards a Potential Biocatalytic Role of Boron

Natálio

Wiese

Brandt

et al. 2017

Chemistry A European J

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Boron's unusual properties inspired major advances in chemistry. In nature, the existence and importance of boron has been fairly explored (e.g. bacterial signaling, plant development) but its role as biological catalyst was never reported. Here, we show that boric acid [B(OH) ] can restore chloroperoxidase activity of Curvularia inaequalis recombinant apo-haloperoxidase's (HPO) in the presence of hydrogen peroxide and chloride ions. Molecular modeling and semi-empirical PM7 calculations support a thermodynamically highly favored (bio)catalytic mechanism similarly to vanadium haloperoxidases (V-HPO) in which [B(OH) ] is assumedly located in apo-HPO's active site and a monoperoxyborate [B(OH) (OOH) ] intermediate is formed and stabilized by interaction with specific active site amino acids leading ultimately to the formation of HOCl. Thus, B(OH) -HPO provides the first evidence towards the future exploitation of boron's role in biological systems.

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confidence: 99%