In vitro reconstitution of the radical S-adenosylmethionine enzyme MqnC involved in the biosynthesis of futalosine-derived menaquinone.

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Abstract

The radical S-adenosylmethionine enzyme MqnC catalyzes conversion of dehypoxanthine futalosine (DHFL) to the unique spiro compound cyclic DHFL in the futalosine pathway for menaquinone biosynthesis. This study describes the in vitro reconstitution of [4Fe-4S] cluster-dependent MqnC activity and identifies the site of abstraction of a hydrogen atom from DHFL by the adenosyl radical.

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Journal

Journal ID (iso-abbrev): Biochemistry

Title: Biochemistry

Publisher: American Chemical Society (ACS)

ISSN (Electronic): 1520-4995

ISSN (Print): 0006-2960

Publication date (Electronic): Jul 09 2013

Volume: 52

Issue: 27

Affiliations

[1 ] Department of Chemistry, Texas A&M University , College Station, Texas 77842, United States.

Article

Mid ID: NIHMS499770

DOI: 10.1021/bi400498d

PMC ID: 3855634

PubMed ID: 23763543

SO-VID: db0f235d-e2b2-4401-8dd8-9bc8918d98e7

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