The crystal structure of [Fe]-hydrogenase reveals the geometry of the active site

Biological formation and consumption of molecular hydrogen (H2) are catalyzed by hydrogenases, of which three phylogenetically unrelated types are known: [NiFe]-hydrogenases, [FeFe]-hydrogenases, and [Fe]-hydrogenase. We present a crystal structure of [Fe]-hydrogenase at 1.75 angstrom resolution, showing a mononuclear iron coordinated by the sulfur of cysteine 176, two carbon monoxide (CO) molecules, and the sp2-hybridized nitrogen of a 2-pyridinol compound with back-bonding properties similar to those of cyanide. The three-dimensional arrangement of the ligands is similar to that of thiolate, CO, and cyanide ligated to the low-spin iron in binuclear [NiFe]- and [FeFe]-hydrogenases, although the enzymes have evolved independently and the CO and cyanide ligands are not found in any other metalloenzyme. The related iron ligation pattern of hydrogenases exemplifies convergent evolution and presumably plays an essential role in H2 activation. This finding may stimulate the ongoing synthesis of catalysts that could substitute for platinum in applications such as fuel cells.     

Voyager 1: energetic ions and electrons in the jovian magnetosphere

The observations of the cosmic-ray subsystem have added significantly to our knowledge of Jupiter's magnetosphere. The most surprising result is the existence of energetic sulfur, sodium, and oxygen nuclei with energies above 7 megaelectron volts per nucleon which were found inside of Io's orbit. Also, significant fluxes of similarly energetic ions reflecting solar cosmic-ray composition were observed throughout the magnetosphere beyond 11 times the radius of Jupiter. It was also found that energetic protons are enhanced by 30 to 70 percent in the active hemisphere. Finally, the first observations were made of the magnetospheric tail in the dawn direction out to 160 Jupiter radii.