Noritake Yasuoka

TL;DR: The crystal structure of the bovine 20S proteasome is determined at 2.75 A resolution and a model of the immunoproteasome was predicted from this constitutive structure.

TL;DR: The X-ray structure of the hydrogenase from Desulfovibrio vulgaris Miyazaki has been solved at 1.8 A resolution and refined to a crystallographic R factor of 0.229, and the most probable candidates for the four ligands, coordinating the Ni-Fe center, have been proposed to be diatomic S=O, C triple bond O and C triple Bond N molecules and one sulfur atom.

TL;DR: The unusual ligand structure found in the oxidized form of D. vulgaris Miyazaki F [NiFe] hydrogenase was confirmed in the reduced form of the enzyme, with the exception that the electron density assigned to the monatomic sulfur bridge had almost disappeared.

TL;DR: The structure of cytochrome c3 from the sulfate-reducing bacterium Desulfovibrio vulgaris Miyazaki has been successfully refined at 1.8 A resolution and the differences in the heme structures and their environments indicate that the four heme groups are non-equivalent.

TL;DR: The frequencies and relative intensities of the CO-related Raman bands indicated that the exogenously added CO is bound to the Ni atom with a bent Ni-C-O structure in solution, in agreement with the refined structure determined by X-ray crystallography.