Azide binding to carbon monoxide dehydrogenase from Clostridium thermoaceticum

Journal Article · Wed Mar 15 04:00:00 EST 1995 · Journal of the American Chemical Society

DOI:https://doi.org/10.1021/ja00115a034· OSTI ID:35478

Kumar, M; Lu, W P; Ragsdale, S W ^[1]; Smith, A; McCracken, J ^[2]

---

1. Univ. of Nebraska, Lincoln, NE (United States)
2. Michigan State Univ., East Lansing, MI (United States)

Carbon monoxide dehydrogenase (CODH) plays a central role in a recently discovered pathway of anaerobic CO and CO{sub 2} fixation. In this communication, the EPR properties of a paramagnetic species that results from azide treatment of reduced CODH are explored. Azide, an inhibitor of CO oxidation, was found to dramatically alter the EPR spectrum of center C that is normally observed for untreated samples under reducing conditions. Electron spin echo envelope modulation (ESEEM) measurements show that azide is bound to the new paramagnetic species. 29 refs., 3 figs.

• Sponsoring Organization: USDOE
• OSTI ID: 35478
• Journal Information: Journal of the American Chemical Society, Journal Name: Journal of the American Chemical Society Journal Issue: 10 Vol. 117; ISSN JACSAT; ISSN 0002-7863
• Country of Publication: United States
• Language: English

Related Subjects

40 CHEMISTRY
AZIDES
CARBON MONOXIDE
CHEMICAL BONDS
ELECTRON SPECTRA
ELECTRON SPIN RESONANCE
ENZYMES
OXIDATION
OXIDOREDUCTASES