Implications of a carboxylate-bound C-cluster structure of carbon monoxide dehydrogenase. Academic Article

abstract

• Seeing the C: Nickel-containing carbon monoxide dehydrogenases reversibly oxidize CO to CO2 at a {[Fe3S4]:[Ni Fe a]} active site known as the C-cluster. Recently reported structures of the enzyme by Jeoung and Dobbek, including those of CO2-bound and OH-bound intermediates, shed new light on the enzyme's catalytic mechanism. This Highlight describes these developments and their implications. (Chemical Equation Presented) 2008 Wiley-VCH Verlag GmbH & Co. KGaA.

authors

• Lindahl, Paul

published proceedings

• Angew Chem Int Ed Engl

author list (cited authors)

• Lindahl, P. A.

citation count

• 26

complete list of authors

• Lindahl, Paul A

publication date

• May 2008

publisher

• Wiley  Publisher

published in

• Angewandte Chemie International Edition  Journal

keywords

• Aldehyde Oxidoreductases
• Bacterial Proteins
• Binding Sites
• Catalysis
• Metalloproteins
• Multienzyme Complexes
• Nickel
• Oxidation-Reduction
• Protein Conformation
• Protein Subunits

PubMed Central ID

• 18404747

Digital Object Identifier (DOI)

• 10.1002/anie.200800223

start page

• 4054

end page

• 4056

volume

• 47

issue

• 22

URL

• http://dx.doi.org/10.1002/anie.200800223