Insights into the mechanistic role of the [Fe4S4] cubane in the A-cluster {[Fe4S4]-(SR)-[NipNid]} of acetyl-coenzyme A synthase. Academic Article

abstract

• Cubane revolution: We have constructed various mutants to probe the role of [Fe4S4] cubane. The results show that [Fe4S4] cubane, which is bridged to a [NipNid] center via Cys509 cysteinate in the A-cluster of acetyl-coenzyme A synthase (see figure), modulates the redox properties of the catalytic metal Nip and stabilizes the low valence of Nip through the {[Fe4S4]-(SR)-Nip} "conjugation system". 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

authors

• Li, Pingwei

published proceedings

• Chembiochem

author list (cited authors)

• Liu, Y. i., Wang, F., Li, P., & Tan, X.

citation count

• 5

complete list of authors

• Liu, Yi||Wang, Feng||Li, Pingwei||Tan, Xiangshi

publication date

• June 2011

publisher

• Wiley  Publisher

published in

• ChemBioChem  Journal

keywords

• Binding Sites
• Coenzyme A Ligases
• Corrinoids
• Ferrous Compounds
• Iron-sulfur Proteins
• Models, Molecular
• Molecular Structure
• Multigene Family
• Nickel

PubMed Central ID

• 21626638

Digital Object Identifier (DOI)

• 10.1002/cbic.201100101

start page

• 1417

end page

• 1421

volume

• 12

issue

• 9

URL

• http%3A%2F%2Fdx.doi.org%2F10.1002%2Fcbic.201100101