Three-dimensional structure of the nickel-containing hydrogenase from Thiocapsa roseopersicina

J Bacteriol. 1991 Apr;173(8):2576-80. doi: 10.1128/jb.173.8.2576-2580.1991.

Abstract

The three-dimensional structure of the nickel-containing hydrogenase from Thiocapsa roseopersicina has been determined at a resolution of 2 nm in the plane and 4 nm in the vertical direction by electron microscopy and computerized image processing on microcrystals of the enzyme. The enzyme forms a large ring-shaped complex containing six each of the large (62-kDa) and small (26-kDa) subunits. The complex is very open, with six well-separated dumbbell-shaped masses surrounding a large cylindrical hole. Each dumbbell is interpreted as consisting of one large and one small subunit.

MeSH terms

  • Electrophoresis, Polyacrylamide Gel
  • Gram-Negative Chemolithotrophic Bacteria / enzymology*
  • Hydrogenase / chemistry*
  • Microscopy, Electron
  • Models, Molecular
  • Molecular Conformation

Substances

  • Hydrogenase