13C nuclear magnetic resonance study of the CO2 activation of ribulosebisphosphate carboxylase from Rhodospirillum rubrum
AUTOR(ES)
O'Leary, Marion H.
RESUMO
Ribulosebisphosphate carboxylase [3-phospho-D-glycerate carboxy-lyase (dimerizing), EC 4.1.1.39] from Rhodospirillum rubrum is activated by CO2 and Mg2+. 13C NMR spectra were determined for the unactivated enzyme and for enzyme that had been activated by 13CO2 and Mg2+. In addition to the expected resonance for H13CO3-/CO32- at 161.8 ppm downfield from tetramethylsilane, the spectrum of the activated enzyme shows a broad resonance at 164.9 ppm. Analogy with previous NMR studies of 13CO2 binding to hemoglobin [Morrow, J. S., Keim, P., Visscher, R. B., Marshall, R. C. & Gurd, F. R. N. (1973) Proc. Natl. Acad. Sci. USA 70, 1414-1418], to myoglobin, and to amino acids [Morrow, J. S., Keim, P. & Gurd, F. R. N. (1974) J. Biol. Chem. 249, 7484-7494] suggests that the CO2 activation of ribulosebisphosphate carboxylase involves formation of a carbamate between an enzyme amino group and CO2.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=383014Documentos Relacionados
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