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. 1979 Feb;76(2):673–675. doi: 10.1073/pnas.76.2.673

13C nuclear magnetic resonance study of the CO2 activation of ribulosebisphosphate carboxylase from Rhodospirillum rubrum

Marion H O'Leary *, Robert J Jaworski *, Fred C Hartman †
PMCID: PMC383014  PMID: 16592618

Abstract

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.

Keywords: photosynthesis, enzymology

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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