Issue 11, 2011
From the journal:

Chemical Communications

Nitric oxide reversibly inhibits Bacillus subtilisoxalate decarboxylase†

Mario E. G. Moral,a   Chingkuang Tu,b   Witcha Imaram,a   Alexander Angerhofer,a   David N. Silvermanbc  and  Nigel G. J. Richards*a  

* Corresponding authors

a Department of Chemistry, University of Florida, Gainesville, USA
E-mail: richards@qtp.ufl.edu
Fax: +1 352 846 2095
Tel: +1 352 392 3601

b Department of Pharmacology & Therapeutics, University of Florida, Gainesville, USA

c Department of Biochemistry & Molecular Biology, University of Florida, Gainesville, USA

Abstract

Membrane inlet mass spectrometry (MIMS) has been employed to assay the catalytic activity of oxalate decarboxylase (OxDC), allowing us to demonstrate that nitric oxide (NO) reversibly inhibits the enzyme under dioxygen-depleted conditions. X-band EPR measurements do not provide any direct evidence for the interaction of NO with either of the Mn(II) centers in OxDC raising the possibility that there is a separate dioxygen-binding pocket in the enzyme.

Graphical abstract: Nitric oxide reversibly inhibits Bacillus subtilisoxalate decarboxylase

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Article information

DOI
https://doi.org/10.1039/C0CC04946H
Article type
Communication
Submitted
13 Nov 2010
Accepted
10 Jan 2011
First published
24 Jan 2011

Chem. Commun., 2011,47, 3111-3113

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Nitric oxide reversibly inhibits Bacillus subtilisoxalate decarboxylase

M. E. G. Moral, C. Tu, W. Imaram, A. Angerhofer, D. N. Silverman and N. G. J. Richards, Chem. Commun., 2011, 47, 3111 DOI: 10.1039/C0CC04946H

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