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

By Xiaoshi Wang

ISBN-10: 3319032356

ISBN-13: 9783319032351

ISBN-10: 3319032364

ISBN-13: 9783319032368

In this thesis, Xiaoshi Wang investigates the functionality and mechanism of a newly came across heme-thiolate peroxygenase, AaeAPO. This enzyme type comes from Agrocybe aegerita and is utilized in the conversion of inert hydrocarbons to alcohols. Xiaoshi's paintings specializes in an extracellular P450 enzyme which isn't restricted in its balance and absence of solubility and consequently is appropriate for frequent commercial use. the writer demonstrates that the peroxygenase catalyzes quite a lot of reactions. every so often the writer even describes very tough modifications in molecules which are hugely inert. Her specified investigations supply a mechanistic framework for the way the peroxygenase catalyzes this sort of huge variety of reactions. a massive spotlight of this thesis is the id of key short-lived intermediates within the catalytic cycle of the peroxygenase, utilizing quick kinetic and spectroscopic tools, in addition to the elucidation of the thermodynamic homes of those high-energy intermediates. This paintings provides new perception into a huge classification of enzymes.

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Additional info for A Novel Heme-Thiolate Peroxygenase AaeAPO and Its Implications for C-H Activation Chemistry

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J. Am. Chem. Soc. 125, 14674–14675 (2003) 75. : X-ray absorption spectroscopic characterization of a cytochrome P450 compound II derivative. Proc. Natl. Acad. Sci. USA 105, 8179–8184 (2008) 76. : Resonance Raman spectroscopy of chloroperoxidase compound II provides direct evidence for the existence of an iron(IV)-hydroxide. Proc. Natl. Acad. Sci. USA 103, 12307–12310 (2006) 77. : Hydrogen atom abstraction by metal-oxo complexes: understanding the analogy with organic radical reactions. Acc. Chem.

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. Proc. Natl. Acad. Sci. USA 102, 16563–16565 (2005) 69. : Observation of the Fe (IV)=O stretching Raman band for a thiolate-ligated heme protein. Compound I of chloroperoxidase. FEBS Lett. 305, 206–208 (1992) 70.

Then, in the so-called rebound step, the iron-bound hydroxyl group captures the incipient carbon radical, resulting in the hydroxylated product and ferric enzyme. Last, the product is released from the active site and completes the cycle. Detailed knowledge of the structural and electronic features of the intermediates are very important for a thorough understanding of the mechanism of heme-thiolate enzyme catalysts. So far, many intermediates have been detected and characterized in the catalytic cycle of porphyrin model complexes, AaeAPO, CPO and CYP enzymes by various biophysical experimental methods [41, 44, 45].

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A Novel Heme-Thiolate Peroxygenase AaeAPO and Its Implications for C-H Activation Chemistry by Xiaoshi Wang


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