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Nitric oxide reversibly inhibits Bacillus subtilis oxalate 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.

SUBMITTER: Moral ME 

PROVIDER: S-EPMC3057162 | biostudies-literature | 2011 Mar

REPOSITORIES: biostudies-literature

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Nitric oxide reversibly inhibits Bacillus subtilis oxalate decarboxylase.

Moral Mario E G ME   Tu Chingkuang C   Imaram Witcha W   Angerhofer Alexander A   Silverman David N DN   Richards Nigel G J NG  

Chemical communications (Cambridge, England) 20110124 11


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. ...[more]

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