Isolation of a stable enzyme.14CO2.Mg2+.carboxyarabinitol bisphosphate complex with ribulosebisphosphate carboxylase from Chromatium vinosum.
AUTOR(ES)
Brown, H M
RESUMO
Higher plant-type ribulosebisphoshate carboxylase from Chromatium vinosum formed a stable, nonexchangeable complex with activator 14CO2 in the presence of Mg2+ and 2-carboxyarabinitol bisphosphate, an analog of the proposed transition-state intermediate. The response of the procaryotic enzyme to this analog was indistinguishable from that of the higher-plant carboxylase, which should permit comparative analysis of the activator site amino acid sequence in the two proteins.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=216512Documentos Relacionados
- Isolation, identification, and synthesis of 2-carboxyarabinitol 1-phosphate, a diurnal regulator of ribulose-bisphosphate carboxylase activity
- Isolation and partial characterization of the major outer membrane protein of Chromatium vinosum.
- Thioredoxin system of the photosynthetic anaerobe Chromatium vinosum.
- Purification and properties of the glutathione reductase of Chromatium vinosum.
- Biological and physicochemical properties of the lipopolysaccharide of Chromatium vinosum.