Open AccessPurification of form L 2 RubisCO from a marine obligately autotrophic hydrogen‐oxidizing bacterium, Hydrogenovibrio marinus strain MH‐110
Author(s) -
Chung Seon Yong,
Yaguchi Toshiaki,
Nishihara Hirofumi,
Igarashi Yasuo,
Kodama Tohru
Publication year - 1993
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1993.tb06142.x
Subject(s) - rubisco , rhodospirillum rubrum , rhodospirillaceae , rhodospirillales , rhodobacter sphaeroides , autotroph , biochemistry , ribulose 1,5 bisphosphate , biology , rhodobacter , bacteria , ribulose , homotetramer , photosynthesis , enzyme , protein subunit , gene , genetics , mutant
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 L 2 ‐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 L 2 ‐form RubisCO of Rhodospirillum rubrum and the L x ‐form RubisCO from Rhodobacter sphaeroides .