Nitric oxide reversibly inhibits Bacillus subtilis oxalate decarboxylase.
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.
Department of Chemistry, University of Florida, Gainesville, FL 32611, USA.
Mario E G
ME
Moral
Chingkuang
C
Tu
Witcha
W
Imaram
Alexander
A
Angerhofer
David N
DN
Silverman
Nigel G J
NG
Richards
D001412:Bacillus subtilis / Q000201:enzymology*; D055162:Biocatalysis; D002262:Carboxy-Lyases / Q000037:antagonists & inhibitors* / Q000378:metabolism; D004578:Electron Spin Resonance Spectroscopy; D008345:Manganese / Q000737:chemistry; D013058:Mass Spectrometry; D009569:Nitric Oxide / Q000737:chemistry*; D011485:Protein Binding; D013997:Time Factors
D009569:Nitric Oxide; D008345:Manganese; D002262:Carboxy-Lyases; C021915:oxalate decarboxylase
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