A Novel Heme-Thiolate Peroxygenase AaeAPO and Its by Xiaoshi Wang

March 9, 2017 | Chemistry | By admin | 0 Comments

By Xiaoshi Wang

In this thesis, Xiaoshi Wang investigates the functionality and mechanism of a newly came across heme-thiolate peroxygenase, AaeAPO. This enzyme classification comes from Agrocybe aegerita and is utilized in the conversion of inert hydrocarbons to alcohols. Xiaoshi's paintings makes a speciality of an extracellular P450 enzyme which isn't constrained in its balance and absence of solubility and for that reason is suitable for common business use. the writer demonstrates that the peroxygenase catalyzes a variety of reactions. every now and then the writer even describes very tricky ameliorations in molecules which are hugely inert. Her distinctive investigations supply a mechanistic framework for the way the peroxygenase catalyzes this sort of huge variety of reactions. an immense spotlight of this thesis is the id of key short-lived intermediates within the catalytic cycle of the peroxygenase, utilizing fast kinetic and spectroscopic equipment, in addition to the elucidation of the thermodynamic houses of those high-energy intermediates. This paintings provides new perception into an enormous category of enzymes.

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Inorg. Chem. 9, 669–683 (2004) 14. : The copper-enzyme family of dopamine β-monooxygenase and peptidylglycine α-hydroxylating monooxygenase: resolving the chemical pathway for substrate hydroxylation. J. Biol. Chem. 281, 3013–3016 (2006) 15. : New insights into copper monooxygenases and peptide amidation: structure, mechanism and function. Cell. Mol. Life Sci. 57, 1236–1259 (2000) 16. R. ) Cytochrome P450: Structure, Mechanism and Biochemistry, 3rd edn. pp. 1–44. Kluwer Academic/Plenum, New York (2004) 17.

Cryotrapped reaction intermediates of cytochrome P450 studied by radiolytic reduction with phosphorus-32. J. Biol. Chem. 276, 11648–11652 (2001) 66. : Evidence for compound I formation in the reaction of cytochrome-P450cam with M-chloroperbenzoic acid. Biochem. Biophys. Res. Co. 201, 1464– 1469 (1994) 67. : Cytochrome P450 compound I: capture, characterization, and C-H bond activation kinetics. Science 330, 933–937 (2010) 68. : X-ray absorption spectroscopy of chloroperoxidase compound I: Insight into the reactive intermediate of P450 chemistry.

Glu183 has been proposed to facilitate Fig. 1 Introduction 5 Fig. 4 Proposed mechanism of CPO compound I formation assisted by glutamic acid and histidine in the active site [30] compound I formation via O–O bond cleavage of a hydroperoxoiron(III) precursor (FeIII–O–OH, so-called compound 0) by supplying a proton during O–O bond scission to form water and compound I. A mechanistic scheme is shown in Fig. 4. Upon replacement of Glu183 the chlorination activity of CPO is reduced [32]. Also, the highest activity of CPO is achieved at acid pH.

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