Details

Autor(en) / Beteiligte

• Drennan, Catherine L.
• Heo, Jongyun
• Sintchak, Michael D.
• Schreiter, Eric
• Ludden, Paul W.

Titel

Life on Carbon Monoxide: X-Ray Structure of Rhodospirillum rubrum Ni-Fe-S Carbon Monoxide Dehydrogenase

Ist Teil von

• Proceedings of the National Academy of Sciences - PNAS, 2001-10, Vol.98 (21), p.11973-11978

Ort / Verlag

United States: National Academy of Sciences

Erscheinungsjahr

2001

Link zum Volltext

Quelle

MEDLINE

Beschreibungen/Notizen

• A crystal structure of the anaerobic Ni-Fe-S carbon monoxide dehydrogenase (CODH) from Rhodospirillum rubrum has been determined to 2.8-Å resolution. The CODH family, for which the R. rubrum enzyme is the prototype, catalyzes the biological oxidation of CO at an unusual Ni-Fe-S cluster called the C-cluster. The Ni-Fe-S C-cluster contains a mononuclear site and a four-metal cubane. Surprisingly, anomalous dispersion data suggest that the mononuclear site contains Fe and not Ni, and the four-metal cubane has the form [NiFe3S 4] and not [Fe4S 4]. The mononuclear site and the four-metal cluster are bridged by means of Cys531and one of the sulfides of the cube. CODH is organized as a dimer with a previously unidentified [Fe4S 4] cluster bridging the two subunits. Each monomer is comprised of three domains: a helical domain at the N terminus, an α/β (Rossmann-like) domain in the middle, and an α/β (Rossmann-like) domain at the C terminus. The helical domain contributes ligands to the bridging [Fe4S 4] cluster and another [Fe4S 4] cluster, the B-cluster, which is involved in electron transfer. The two Rossmann domains contribute ligands to the active site C-cluster. This x-ray structure provides insight into the mechanism of biological CO oxidation and has broader significance for the roles of Ni and Fe in biological systems.