A redox hydrogel with an apparent electron diffusion coefficient (D(app)) of (5.8 +/- 0.5) x 10(-)(6) cm(2) s(-)(1) is described. The order of magnitude increase in D(app) relative to previously studied redox hydrogels results from the tethering of redox centers to the backbone of the cross-linked redox polymer backbone through 13 atom spacer arms. The long and flexible tethers allow the redox centers to sweep electrons from large-volume elements and to collect electrons of glucose oxidase efficiently. The spacer arms make the collection of electrons from glucose oxidase so efficient that glucose is electrooxidized already at -0.36 V versus Ag/AgCl, the reversible potential of the redox potential of the FAD/FADH(2) centers of the enzyme at pH 7.2. The limiting current density of 1.15 mA cm(-)(2) is reached at a potential as low as -0.1 V versus Ag/AgCl. The novel redox center of the polymer is a tris-dialkylated N,N'-biimidazole Os(2+/3+) complex. Its redox potential, -0.195 V versus Ag/AgCl, is 0.8 V reducing relative to that of Os(bpy)(2+/3+), its 2,2'-bipyridine analogue.

We report the temperature, pH, glucose concentration, NaCl concentration, and operating atmosphere dependence of the power output of a compartment-less miniature glucose-O(2) biofuel cell, comprised only of two bioelectrocatalyst-coated carbon fibers, each of 7 micro m diameter and 2 cm length (Mano, N.; Mao, F.; Heller, A. J. Am. Chem. Soc. 2002, 124, 12962). The bioelectrocatalyst of the anode consists of glucose oxidase from Aspergillus niger electrically "wired" by polymer I, having a redox potential of -0.19 V vs Ag/AgCl. That of the cathode consists of bilirubin oxidase from Trachyderma tsunodae "wired" by polymer II having a redox potential of +0.36 V vs Ag/AgCl (Mano, N.; Kim, H.-H.; Zhang, Y.; Heller, A. J. Am. Chem. Soc. 2002, 124, 6480. Mano, N.; Kim, H.-H.; Heller, A. J. Phys. Chem. B 2002, 106, 8842). Implantation of the fibers in the grape leads to an operating biofuel cell producing 2.4 micro W at 0.52 V.

Catalytic four-electron reduction of O to water is one of the most extensively studied electrochemical reactions due to O exceptional availability and high O/HO redox potential, which may in particular allow highly energetic reactions in fuel cells. To circumvent the use of expensive and inefficient Pt catalysts, multicopper oxidases (MCOs) have been envisioned because they provide efficient O reduction with almost no overpotential. MCOs have been used to elaborate enzymatic biofuel cells (EBFCs), a subclass of fuel cells in which enzymes replace the conventional catalysts. A glucose/O EBFC, with a glucose oxidizing anode and a O reducing MCO cathode, could become the in vivo source of electricity that would power sometimes in the future integrated medical devices. This review covers the challenges and advances in the electrochemistry of MCOs and their use in EBFCs with a particular emphasis on the last 6 years. First basic features of MCOs and EBFCs are presented. Clues provided by electrochemistry to understand these enzymes and how they behave once connected at electrodes are described. Progresses realized in the development of efficient biocathodes for O reduction relying both on direct and mediated electron transfer mechanism are then discussed. Some implementations in EBFCs are finally presented.

We report the electroreduction of O(2) to water under physiological conditions (pH 7.4, 0.15 M NaCl, 37.5 degrees C) at a current density of 5 mA cm(-2) and at a potential only 0.18 V reducing versus that of the reversible O(2)/H(2)O electrode at pH 7.4. The immobilized electrocatalyst enabling the reduction is the electrostatic adduct of bilirubin oxidase from Myrothecium verrucaria, a polyanion at pH >4.1, and the polycationic redox copolymer of polyacrylamide and poly (N-vinylimidazole) complexed with [Os (4,4'-dichloro-2,2'-bipyridine)(2)Cl](+/2+), cross-linked on carbon cloth. The current density of the rotating electrodes was O(2) transport limited up to 8.8 mA cm(-2); their kinetic limit was reached at 9.1 mA cm(-2). The operational life of the electrodes depended on their angular velocity, which defined not only the current density but also the mechanical shear stress stripping the electrocatalyst. When the electrodes were rotated at 300 rpm and were poised at -256 mV versus the potential of the reversible O(2)/H(2)O electrode, their 2.4 mA cm(-2) initial current density decreased to 1.3 mA cm(-2) after 6 days of continuous operation at 37.5 degrees C.

A carbon fiber having a terminal glucose oxidizing microanode and an O2 reducing microcathode is propelled at the water-O2 interface. The electron current in the fiber is accompanied by a flux of hydrated protons that is so fast at the solution-air interface, where the viscous drag is small, that the fiber's velocity is 1 cm s-1.

A glucose-O2 biofuel cell, consisting only of two electrocatalyst coated 7-mum diameter, 2-cm long carbon fibers is reported. The cell operated continuously at 0.52 V at 37 degrees C in a physiological buffer solution for a week, producing 1.9 muW during the first and 1.0 muW during the last day, generating in the period 0.9 J of electrical energy while passing a charge of 1.7 C. If a similar dimension zinc fiber were utilized in a battery at 100% current efficiency, only 0.016 C would have been generated.

O2 was electroreduced to water, at a true-surface-area-based current density of 0.5 mA cm-2, at 37 degrees C and at pH 5 on a "wired" laccase bioelectrocatalyst-coated carbon fiber cathode. The polarization (potential vs the reversible potential of the O2 /H2O half-cell in the same electrolyte) of the cathode was only -0.07 V, approximately one-fifth of the -0.37 V polarization of a smooth platinum fiber cathode, operating in its optimal electrolyte, 0.5 M H2SO4. The bioelectrocatalyst was formed by "wiring" laccase to carbon through an electron conducting redox hydrogel, its redox functions tethered through long and flexible spacers to its cross-linked and hydrated polymer. Incorporation of the tethers increased the apparent electron diffusion coefficient 100-fold to (7.6 +/- 0.3) x 10-7 cm 2 s-1. A miniature single-compartment glucose-O2 biofuel cell made with the novel cathode operated optimally at 0.88 V, the highest operating voltage for a compartmentless miniature fuel cell.

The first enzyme-based catalyst that is superior to platinum in the four-electron electroreduction of oxygen to water is reported. The smooth Pt cathode reached half and 90% of the mass transport-limited current density at respective overpotentials of -0.4 and -0.58 V in 0.5 M sulfuric acid, and only at even higher overpotentials in pH 7.2 phosphate buffer. In contrast, the smooth "wired" bilirubin oxidase cathode reached half and 90% of the mass transport-limited current density at respective overpotentials as low as -0.2 and -0.25 V. The mass transport-limited current density for the smooth "wired" enzyme cathode in PBS was twice that with smooth Pt in 0.5 M sulfuric acid. Under 1 atm O2 pressure, O2 was electroreduced to water on a polished carbon cathode, coated with the "wired" BOD film, in pH 7.2 saline buffer (PBS) at an overpotential of -0.31 V at a current density of 9.5 mA cm-2. At the same overpotential, the current density of the polished platinum cathode in 0.5 M H2SO4 was 16-fold lower, only 0.6 mA cm-2.