We demonstrate the use of individual semiconducting single-wall carbon nanotubes as versatile biosensors. Controlled attachment of the redox enzyme glucose oxidase (GOx) to the nanotube sidewall is achieved through a linking molecule and is found to induce a clear change of the conductance. The enzyme-coated tube is found to act as a pH sensor with large and reversible changes in conductance upon changes in pH. Upon addition of glucose, the substrate of GOx, a steplike response can be monitored in real time, indicating that our sensor is also capable of measuring enzymatic activity at the level of a single nanotube. This first demonstration of nanotube-based biosensors provides a new tool for enzymatic studies and opens the way to biomolecular diagnostics.

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We demonstrate the use of individual single-walled carbon nanotubes (SWNTs) as nanoelectrodes for electrochemistry. SWNTs were contacted by nanolithography, and cyclic voltammetry was performed in aqueous solutions. Interestingly, metallic and semiconducting SWNTs yielded similar steady-state voltammetric curves. We clarify this behavior through a model that considers the electronic structure of the SWNTs. Interfacial electron transfer to the SWNTs is observed to be very fast but can nonetheless be resolved due to the nanometer critical dimension of SWNTs. These studies demonstrate the potential of using a SWNT as a model carbon nanoelectrode for electrochemistry.

The nickel-iron hydrogenase from Chromatium vinosum adsorbs at a pyrolytic graphite edge-plane (PGE) electrode and catalyzes rapid interconversion of H(+)((aq)) and H(2) at potentials expected for the half-cell reaction 2H(+) right arrow over left arrow H(2), i.e., without the need for overpotentials. The voltammetry mirrors characteristics determined by conventional methods, while affording the capabilities for exquisite control and measurement of potential-dependent activities and substrate-product mass transport. Oxidation of H(2) is extremely rapid; at 10% partial pressure H(2), mass transport control persists even at the highest electrode rotation rates. The turnover number for H(2) oxidation lies in the range of 1500-9000 s(-)(1) at 30 degrees C (pH 5-8), which is significantly higher than that observed using methylene blue as the electron acceptor. By contrast, proton reduction is slower and controlled by processes occurring in the enzyme. Carbon monoxide, which binds reversibly to the NiFe site in the active form, inhibits electrocatalysis and allows improved definition of signals that can be attributed to the reversible (non-turnover) oxidation and reduction of redox centers. One signal, at -30 mV vs SHE (pH 7.0, 30 degrees C), is assigned to the [3Fe-4S](+/0) cluster on the basis of potentiometric measurements. The second, at -301 mV and having a 1. 5-2.5-fold greater amplitude, is tentatively assigned to the two [4Fe-4S](2+/+) clusters with similar reduction potentials. No other redox couples are observed, suggesting that these two sets of centers are the only ones in CO-inhibited hydrogenase capable of undergoing simple rapid cycling of their redox states. With the buried NiFe active site very unlikely to undergo direct electron exchange with the electrode, at least one and more likely each of the three iron-sulfur clusters must serve as relay sites. The fact that H(2) oxidation is rapid even at potentials nearly 300 mV more negative than the reduction potential of the [3Fe-4S](+/0) cluster shows that its singularly high equilibrium reduction potential does not compromise catalytic efficiency.