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Photoreductive path of carbon fixation in green plant photosynthesis. Reaction pathway of six-carbon ribulose 1,5-bisphosphate carboxylation adduct intermediate

Authors :
Karen A. Butcher
Francis K. Fong
Source :
Biochemical and Biophysical Research Communications. 142:732-737
Publication Year :
1987
Publisher :
Elsevier BV, 1987.

Abstract

In this paper we examine the six-carbon intermediate pathway of ribulose 1,5-bisphosphate (RuBP) carboxylation reaction in photosynthesis. Based on the observed reactions of purified RuBP carboxylase, mechanisms are described for carbon dioxide assimilation leading to the hydrolytic splitting of the six-carbon intermediate to two enzyme-bound glycerate-3-P (3-PGA) molecules. It is concluded that, under photosynthetic conditions, the reduction of enzyme-bound NADP+ by the chlorophyll is responsible for the rapid carboxylase turnover rate given by the lifetime, τ L = 0.4 s , which is nearly two orders of magnitude shorter than the corresponding value, τ D = 11 ± 3 s , for the dark decay of enzyme-bound RuBP. The nocturnal inhibition and photoactivation of RuBP carboxylation are described in terms of the reversible ligh-dark cycles of the NADP + NADPH redox couple and endogenous changes that accompany the 2-carboxy-D-arabinitoll-phosphate binding to the enzyme active site.

Details

ISSN :
0006291X
Volume :
142
Database :
OpenAIRE
Journal :
Biochemical and Biophysical Research Communications
Accession number :
edsair.doi.dedup.....3a2451b82217234e0d5d666d0be142be
Full Text :
https://doi.org/10.1016/0006-291x(87)91475-6