Reduction and methyl transfer kinetics of the alpha subunit from acetyl coenzyme a synthase. Academic Article

abstract

• Stopped-flow was used to evaluate the methylation and reduction kinetics of the isolated alpha subunit of acetyl-Coenzyme A synthase from Moorella thermoacetica. This catalytically active subunit contains a novel Ni-X-Fe4S4 cluster and a putative unidentified n = 2 redox site called D. The D-site must be reduced for a methyl group to transfer from a corrinoid-iron-sulfur protein, a key step in the catalytic synthesis of acetyl-CoA. The Fe4S4 component of this cluster is also redox active, raising the possibility that it is the D-site or a portion thereof. Results presented demonstrate that the D-site reduces far faster than the Fe4S4 component, effectively eliminating this possibility. Rather, this component may alter catalytically important properties of the Ni center. The D-site is reduced through a pathway that probably does not involve the Fe4S4 component of this active-site cluster.

authors

• Lindahl, Paul

published proceedings

• J Am Chem Soc

author list (cited authors)

• Tan, X., Sewell, C., Yang, Q., & Lindahl, P. A.

citation count

• 39

complete list of authors

• Tan, Xiangshi||Sewell, Christopher||Yang, Qingwu||Lindahl, Paul A

publication date

• January 2003

publisher

• American Chemical Society (ACS)  Publisher

published in

• Journal of the American Chemical Society  Journal

keywords

• Acetate-coa Ligase
• Bacterial Proteins
• Cloning, Molecular
• Clostridium
• Escherichia Coli
• Iron-sulfur Proteins
• Kinetics
• Methylation
• Methyltransferases
• Oxidation-Reduction

PubMed Central ID

• 12517128

Digital Object Identifier (DOI)

• 10.1021/ja028442t

start page

• 318

end page

• 319

volume

• 125

issue

• 2

URL

• http://dx.doi.org/10.1021/ja028442t