Q.What conditions enable Rubirco to function as an oxygenase? Explain the ensuing process.
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Start your 14-day free trial to unlock the full solution →RuBisCO switches to its oxygenase role whenever oxygen is relatively abundant compared to carbon dioxide at its active site, driving the wasteful photorespiration pathway instead of normal CO2 fixation.
RuBisCO, more fully called RuBP carboxylase-oxygenase, earns that full name because its active site is able to bind both carbon dioxide and oxygen. Although the enzyme has a considerably greater affinity for CO2 than for O2, the two gases genuinely compete for the same active site, so which one actually binds at any given moment depends on their relative concentrations rather than on affinity alone.
In C3 plants, where there is no mechanism to keep CO2 concentrated at the site of RuBisCO, some O2 inevitably does bind, and whenever it does, CO2 fixation is correspondingly reduced. When O2 binds instead of CO2, RuBP is not converted into two molecules of PGA as it would be during normal carboxylation. Instead, it is converted into one molecule of phosphoglycerate together with one molecule of phosphoglycolate, a 2-carbon compound — this alternative route is called photorespiration. …
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