Purification of form L2 RubisCO from a marine obligately autotrophic hydrogen-oxidizing bacterium, Hydrogenovibrio marinus strain MH-110.
Ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO) was purified from an obligately autotrophic hydrogen-oxidizing bacterium, Hydrogenovibrio marinus MH-110. The protein has a M(r) value of approximately 110,000, and is composed of two identical subunits of 55,000. To our knowledge, the existence of L2-form RubisCO in a chemolithoautotrophic bacterium is first reported in this paper. The N-terminal amino acid sequence determination of the purified enzyme showed high homology with those of the L2-form RubisCO of Rhodospirillum rubrum and the Lx-form RubisCO from Rhodobacter sphaeroides.
Chung
S Y
SY
Department of Agricultural Chemistry, University of Tokyo, Japan.
Yaguchi
T
T
Nishihara
H
H
Igarashi
Y
Y
Kodama
T
T
D000595:Amino Acid Sequence; D002245:Carbon Dioxide / Q000378:metabolism; D006859:Hydrogen / Q000378:metabolism; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010084:Oxidation-Reduction; D011487:Protein Conformation; D012242:Rhodobacter sphaeroides / Q000201:enzymology / Q000235:genetics; D012247:Rhodospirillum rubrum / Q000201:enzymology / Q000235:genetics; D012273:Ribulose-Bisphosphate Carboxylase / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification*; D017386:Sequence Homology, Amino Acid; D014737:Vibrionaceae / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism
D002245:Carbon Dioxide; D006859:Hydrogen; D012273:Ribulose-Bisphosphate Carboxylase