The organometallic active site of [Fe]hydrogenase: models and entatic states. Academic Article

abstract

• The simple organometallic, (mu-S(2))Fe(2)(CO)(6), serves as a precursor to synthetic analogues of the chemically rudimentary iron-only hydrogenase enzyme active site. The fundamental properties of the (mu-SCH(2)CH(2)CH(2)S)[Fe(CO)(3)](2) compound, including structural mobility and regioselectivity in cyanidecarbon monoxide substitution reactions, relate to the enzyme active site in the form of transition-state structures along reaction paths rather than ground-state structures. Even in the absence of protein-based active-site organization, the ground-state structural model complexes are shown to serve as hydrogenase enzyme reaction models, H(2) uptake and H(2) production, with the input of photo- or electrochemical energy, respectively.

authors

• Darensbourg, Marcetta

published proceedings

• Proc Natl Acad Sci U S A

altmetric score

• 6

author list (cited authors)

• Darensbourg, M. Y., Lyon, E. J., Zhao, X., & Georgakaki, I. P.

citation count

• 260

complete list of authors

• Darensbourg, Marcetta Y||Lyon, Erica J||Zhao, Xuan||Georgakaki, Irene P

publication date

• April 2003

publisher

• Proceedings of the National Academy of Sciences  Publisher

published in

• Proceedings of the National Academy of Sciences of the United States of America  Journal

keywords

• Binding Sites
• Hydrogen
• Hydrogenase
• Iron-sulfur Proteins
• Kinetics
• Models, Molecular
• Organometallic Compounds
• Protein Structure, Secondary

PubMed Central ID

• 12642671

Digital Object Identifier (DOI)

• 10.1073/pnas.0536955100

URI

• https://hdl.handle.net/1969.1/184731

start page

• 3683

end page

• 3688

volume

• 100

issue

• 7

URL

• http://dx.doi.org/10.1073/pnas.0536955100

user-defined tag

• 7 Affordable and Clean Energy