Work

Nitric oxide reversibly inhibits Bacillus subtilis oxalate decarboxylase

Year: 2011

Type: article

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.

Source: Chemical Communications

DOI: 10.1039/c0cc04946h

Authors: Mario E. G. Moral, Chingkuang Tu, Witcha Imaram, Alexander Angerhofer, David N. Silverman, Nigel G. J. Richards

Institution: University of Florida

Language: English

Topic: Metal-Catalyzed Oxygenation Mechanisms

Subfield: Inorganic Chemistry

Field: Chemistry

Domain: Physical Sciences

Open Access status: green

Funders: National Institute of General Medical Sciences, National Institute of Diabetes and Digestive and Kidney Diseases

Awards: Biochemical Studies of Oxalate Decarboxylase, G4646436960, Catalytic Mechanism of Carbonic Anhydrase, G6056057276, Biochemical Studies of Oxalate Decarboxylase