Three-dimensional structure of the nickel-containing hydrogenase from Thiocapsa roseopersicina.
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.
Sherman
M B
MB
Institute of Crystallography, USSR Academy of Sciences, Moscow.
Orlova
E V
EV
Smirnova
E A
EA
Hovmöller
S
S
Zorin
N A
NA
D004591:Electrophoresis, Polyacrylamide Gel; D006091:Gram-Negative Chemolithotrophic Bacteria / Q000201:enzymology*; D006864:Hydrogenase / Q000737:chemistry*; D008854:Microscopy, Electron; D008958:Models, Molecular; D008968:Molecular Conformation
D006864:Hydrogenase