Formation of hexacoordinate Mn(III) in Bacillus subtilis oxalate decarboxylase requires catalytic turnover

Zhu, Wen, Wilcoxen, Jarett, Britt, R. David and Richards, Nigel G. J. ORCID: https://orcid.org/0000-0002-0375-0881 2016. Formation of hexacoordinate Mn(III) in Bacillus subtilis oxalate decarboxylase requires catalytic turnover. Biochemistry 55 (3) , pp. 429-434. 10.1021/acs.biochem.5b01340

Full text not available from this repository.

Abstract

Oxalate decarboxylase (OxDC) catalyzes the disproportionation of oxalic acid monoanion into CO2 and formate. The enzyme has long been hypothesized to utilize dioxygen to form mononuclear Mn(III) or Mn(IV) in the catalytic site during turnover. Recombinant OxDC, however, contains only tightly bound Mn(II), and direct spectroscopic detection of the metal in higher oxidation states under optimal catalytic conditions (pH 4.2) has not yet been reported. Using parallel mode electron paramagnetic resonance spectroscopy, we now show that substantial amounts of Mn(III) are indeed formed in OxDC, but only in the presence of oxalate and dioxygen under acidic conditions. These observations provide the first direct support for proposals in which Mn(III) removes an electron from the substrate to yield a radical intermediate in which the barrier to C–C bond cleavage is significantly decreased. Thus, OxDC joins a small list of enzymes capable of stabilizing and controlling the reactivity of the powerful oxidizing species Mn(III).

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Chemistry
Subjects:	Q Science > QD Chemistry
Publisher:	American Chemical Society
ISSN:	0006-2960
Date of Acceptance:	7 January 2016
Last Modified:	01 Nov 2022 09:22
URI:	https://orca.cardiff.ac.uk/id/eprint/87726

Citation Data

Cited 16 times in Scopus. View in Scopus. Powered By Scopus® Data

Actions (repository staff only)

Edit Item