Determinants of Substrate Specificity and the Role of Metal in the Reactions of Ribulosebisphosphate Carboxylase/Oxygenase
Author(s) -
John P. Pierce
Publication year - 1986
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.81.4.943
Subject(s) - oxygenase , rubisco , pyruvate carboxylase , chemistry , substrate (aquarium) , substrate specificity , biochemistry , biophysics , enzyme , biology , ecology
Recent studies have provided a fairly detailed view of the various intermediates involved in the reactions of ribulosebisphosphate carboxylase and the manner in which the catalytically essential metal atom might catalyze their interconversions. A better understanding of how the enzyme distinguishes between its alternate substrates, CO(2) and O(2), has also emerged. The results of these studies should prove useful in anticipating possible ways in which the enzyme's substrate specificity might be manipulated. Together, the techniques that are described constitute a powerful methodology for more refined experimentation aimed at understanding the curious reactivities of ribulosebisphosphate carboxylase.
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