Issue 11, 2011

Nitric oxide reversibly inhibits Bacillus subtilisoxalate decarboxylase

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

Supplementary files

Article information

Article type
Communication
Submitted
13 Nov 2010
Accepted
10 Jan 2011
First published
24 Jan 2011

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

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

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements