Chloroperoxidase‐Catalyzed Achmatowicz Rearrangements

Daniel Thiel; Fabian Blume; Christina Jäger; Jan Deska

doi:10.1002/ejoc.201800333

Chloroperoxidase‐Catalyzed Achmatowicz Rearrangements

Daniel Thiel, Fabian Blume, Christina Jäger, Jan Deska

Research output: Contribution to journal › Article › Scientific › peer-review

5 Citations (Scopus)

96 Downloads (Pure)

Abstract

Chloroperoxidase from Caldariomyces fumago catalyzes the selective oxidation of furfuryl alcohols in an Achmatowicz‐type ring expansion. In combination with glucose oxidase as oxygen‐activating biocatalyst, a purely enzymatic, aerobic protocol for the synthesis of 6‐hydroxypyranone building blocks is obtained. Thanks to an only modest stereochemical bias of the oxygenating heme protein, optically active alcohols of either configuration are converted without a significant mismatch opening up opportunities for enantioselective multienzymatic cascades. Balancing the oxidase‐driven aerobic activation, extended enzyme half‐lives and productive conversion of poorly soluble and slowly reacting substrates can be achieved with high yields of the six‐membered O‐heterocycles.

Original language	English
Pages (from-to)	2717-2725
Number of pages	9
Journal	European Journal of Organic Chemistry
Volume	20
DOIs	https://doi.org/10.1002/ejoc.201800333
Publication status	Published - 7 Jun 2018
MoE publication type	A1 Journal article-refereed

Keywords

enzyme catalysis
peroxidases
ring expansion
heterocycles
furan

Access to Document

10.1002/ejoc.201800333

EJOC2018Accepted author manuscript, 941 KBLicence: Unspecified

Fingerprint Dive into the research topics of 'Chloroperoxidase‐Catalyzed Achmatowicz Rearrangements'. Together they form a unique fingerprint.

Projects

1 Active

Beyond Biosynthesis: Enzymes as Catalysts in Non-natural Synthetic Transformations

Blume, F., Jäger, C., Deska, J., Naapuri, J., Liu, Y., Kiefer, A. & Wagner, P.

01/09/2016 → 31/03/2021

Project: Academy of Finland: Other research funding

Equipment

Bioeconomy Research Infrastructure

Jukka Seppälä (Manager)

School of Chemical Engineering

Facility/equipment: Facility

Cite this

Thiel, D., Blume, F., Jäger, C., & Deska, J. (2018). Chloroperoxidase‐Catalyzed Achmatowicz Rearrangements. European Journal of Organic Chemistry, 20, 2717-2725. https://doi.org/10.1002/ejoc.201800333

@article{c75cd09a29bd4d51986ff043c111fca5,

title = "Chloroperoxidase‐Catalyzed Achmatowicz Rearrangements",

abstract = "Chloroperoxidase from Caldariomyces fumago catalyzes the selective oxidation of furfuryl alcohols in an Achmatowicz‐type ring expansion. In combination with glucose oxidase as oxygen‐activating biocatalyst, a purely enzymatic, aerobic protocol for the synthesis of 6‐hydroxypyranone building blocks is obtained. Thanks to an only modest stereochemical bias of the oxygenating heme protein, optically active alcohols of either configuration are converted without a significant mismatch opening up opportunities for enantioselective multienzymatic cascades. Balancing the oxidase‐driven aerobic activation, extended enzyme half‐lives and productive conversion of poorly soluble and slowly reacting substrates can be achieved with high yields of the six‐membered O‐heterocycles.",

keywords = "enzyme catalysis, peroxidases, ring expansion, heterocycles, furan",

author = "Daniel Thiel and Fabian Blume and Christina J{\"a}ger and Jan Deska",

year = "2018",

month = jun,

day = "7",

doi = "10.1002/ejoc.201800333",

language = "English",

volume = "20",

pages = "2717--2725",

journal = "European Journal of Organic Chemistry",

issn = "1434-193X",

publisher = "WILEY-BLACKWELL",

}

TY - JOUR

T1 - Chloroperoxidase‐Catalyzed Achmatowicz Rearrangements

AU - Thiel, Daniel

AU - Blume, Fabian

AU - Jäger, Christina

AU - Deska, Jan

PY - 2018/6/7

Y1 - 2018/6/7

N2 - Chloroperoxidase from Caldariomyces fumago catalyzes the selective oxidation of furfuryl alcohols in an Achmatowicz‐type ring expansion. In combination with glucose oxidase as oxygen‐activating biocatalyst, a purely enzymatic, aerobic protocol for the synthesis of 6‐hydroxypyranone building blocks is obtained. Thanks to an only modest stereochemical bias of the oxygenating heme protein, optically active alcohols of either configuration are converted without a significant mismatch opening up opportunities for enantioselective multienzymatic cascades. Balancing the oxidase‐driven aerobic activation, extended enzyme half‐lives and productive conversion of poorly soluble and slowly reacting substrates can be achieved with high yields of the six‐membered O‐heterocycles.

AB - Chloroperoxidase from Caldariomyces fumago catalyzes the selective oxidation of furfuryl alcohols in an Achmatowicz‐type ring expansion. In combination with glucose oxidase as oxygen‐activating biocatalyst, a purely enzymatic, aerobic protocol for the synthesis of 6‐hydroxypyranone building blocks is obtained. Thanks to an only modest stereochemical bias of the oxygenating heme protein, optically active alcohols of either configuration are converted without a significant mismatch opening up opportunities for enantioselective multienzymatic cascades. Balancing the oxidase‐driven aerobic activation, extended enzyme half‐lives and productive conversion of poorly soluble and slowly reacting substrates can be achieved with high yields of the six‐membered O‐heterocycles.

KW - enzyme catalysis

KW - peroxidases

KW - ring expansion

KW - heterocycles

KW - furan

U2 - 10.1002/ejoc.201800333

DO - 10.1002/ejoc.201800333

M3 - Article

VL - 20

SP - 2717

EP - 2725

JO - European Journal of Organic Chemistry

JF - European Journal of Organic Chemistry

SN - 1434-193X

ER -