6 molecules of 14^CO2 were introduced into chlorella algae.how many molecules of PGA must be radioactive??

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Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco; EC 4.1.1.39) catalyzes the addition of gaseous carbon dioxide to ribulose-1,5-bisphosphate (RuBP), generating two molecules of 3-phosphoglyceric acid (3-PGA), and is thus the key enzyme in CO2 assimilation. Rubsico is capable of a competing oxygenation reaction, which generates one molecule of 3-PGA and one of 2-phosphoglycolate from RuBP. In Chlamydomonas as in higher plants, the enzyme is a hexadecamer composed of eight large subunits (LS) and eight small subunits (SS), encoded by a single chloroplast gene (rbcL) and two adjacent nuclear genes (RBCS1/2), respectively. The number of the RBCS genes varies among plants but generally constitutes a small multigene family. Rubisco is mainly localized to the pyrenoid in Chlamydomonas.

Because of its high abundance and central metabolic role, Rubisco has been studied in many cellular contexts. Its high abundance necessitates a considerable diversion of amino acids and energy to its synthesis, and the many physiological stimuli that impinge upon the regulation of photosynthesis, require that Rubisco abundance and activity be controlled. Thus, Rubisco is discussed in several other chapters of this volume. The photorespiratory glycolate pathway, which is initiated through Rubisco oxygenase activity, is discussed in more detail in Chapter 8. This same chapter also discusses the carbon concentrating mechanism and how Rubisco may access its substrates under different growth conditions, particularly limiting CO2, whereas Chapter 7 discusses relevance of Rubisco to hydrogen production. Chapter 29 discusses the translational regulation of LS synthesis in response to SS limitation and oxidative stress; topics which are summarized in section VII. Rubisco is also mentioned in the context of nutrient stress and transition metal deficiency, where it is subject to repression; these are referred to in section VI. Rubisco proteolysis is discussed in Chapter 19.

While Rubisco has been studied in many organisms, and thousands of rbcL genes have been sequenced for phylogenetic purposes (Kapralov and Filatov, 2007), Chlamydomonas has been particularly useful for several reasons. First, the rbcL gene can be readily manipulated by chloroplast transformation, leading to facile structure-function analyses. Second, the two RBCS genes are tightly linked and mutants exist with a deletion covering both. This is thus the only eukaryote for which there are mutants that stably and totally lack RBCS expression (Khrebtukova and Spreitzer, 1996; Dent et al., 2005). Third, culture conditions can be changed rapidly and uniformly. This allows a relatively uniform population to be examined for Rubisco regulation under a variety of stress conditions. This chapter focuses on studies in Chlamydomonas, while other aspects of Rubisco have been reviewed elsewhere. These include its potential to increase CO2 storage in trees and diatoms (Millard et al., 2007; Roberts et al., 2007), choice of model system for studying Rubisco compartmentalization in C4 plants (Brown et al., 2005), and a series of reviews on Rubisco activity, assembly, and manipulation

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