Raman spectroscopy of charge transfer interactions between single wall carbon nanotubes and [FeFe] hydrogenase.
We report a Raman spectroscopy study of charge transfer interactions in complexes formed by single-walled carbon nanotubes (SWNTs) and [FeFe] hydrogenase I (CaHydI) from Clostridium acetobutylicum. The choice of Raman excitation wavelength and sample preparation conditions allows differences to be observed for complexes involving metallic (m) and semiconducting (s) species. Adsorbed CaHydI can reversibly inject electronic charge into the LUMOs of s-SWNTs, while charge can be injected and removed from m-SWNTs at lower potentials just above the Fermi energy. Time-dependent enzymatic assays demonstrated that the reduced and oxidized forms of CaHydI are deactivated by oxygen, but at rates that varied by an order of magnitude. The time evolution of the oxidative decay of the CaHydI activity reveals different time constants when complexed with m-SWNTs and s-SWNTs. The correlation of enzymatic assays with time-dependent Raman spectroscopy provides a novel method by which the charge transfer interactions may be investigated in the various SWNT-CaHydI complexes. Surprisingly, an oxidized form of CaHydI is apparently more resistant to oxygen deactivation when complexed to m-SWNTs rather than s-SWNTs.
Blackburn
Jeffrey L
JL
National Renewable Energy Laboratory, Material Science, 16253 Denver West Parkway, Golden, Colorado, 80401, USA.
Svedruzic
Drazenka
D
McDonald
Timothy J
TJ
Kim
Yong-Hyun
YH
King
Paul W
PW
Heben
Michael J
MJ
D003013:Clostridium / Q000201:enzymology; D006864:Hydrogenase / Q000737:chemistry* / Q000378:metabolism*; D007477:Ions / Q000737:chemistry; D007506:Iron-Sulfur Proteins / Q000737:chemistry* / Q000378:metabolism*; D007700:Kinetics; D037742:Nanotubes, Carbon / Q000737:chemistry*; D013059:Spectrum Analysis, Raman
D007477:Ions; D007506:Iron-Sulfur Proteins; D037742:Nanotubes, Carbon; C118830:iron hydrogenase; D006864:Hydrogenase