Cupreine structure

Figure 13.2 Structural features of cinchona alkaloid molecules (QN, quinine QD, quinidine CN, cinchonine CD, cinchonidine CPN, cupreine CPD, cupreidine).

Contents U.Weser Structural Aspects and Biochemical Function of Erythro-cuprein. - R.R.Crichton Ferritin. -M.Llinas Metal-Polypeptide Interactions The Conformational State of Iron Proteins. - F.L.Siegel Calcium-Binding Proteins. 

Since the discovery of superoxide dismutase (SOD) by McCord and Fridovich (Ml9), increasing numbers of papers have been published concerning the structural and functional aspects of this enzyme. Historically, a variety of SODs were reported as copper-containing proteins hemocuprein from bovine blood (M2), hepatocuprein from horse liver (M28), cerebrocuprein from human brain (P10), and ery throcupurein from human and beef erythrocytes (M9). Carrico and Deutsch (C2) gave the name cytocuprein to these proteins because the cupreins from various organs were found to be essentially identical. Cytocuprein was found to... 

Our knowledge of the structural properties and enzymic function of a large number of copper proteins has accumulated during the last few decades. The main results have been comprehensively reviewed 1—4) or presented at symposia (5—54). This survey is devoted to erythro-cuprein, one of the most actively studied copper proteins. Erythrocu-prein is sometimes called haemocuprein, hepatocuprein, cerebrocuprein, cytocuprein, or erythro-cupro-zinc protein. Alternatively, the name superoxide dismutase has been suggested as descriptive of its activity the enzyme-catalyzed disproportionation of anionic monovalent superoxide radicals. However, whether or not the enzymic reaction is specific for Oi- still needs to be investigated1). Thus, the name erythrocuprein is used throughout this review. 

Since the scope of the reaction with respect to the electrophile vras limited to trifluoropyruvate, in 2006 Deng and coworkers searched for a more efficient catalyst for the Friedel-Crafts hydro)grallgrlation of indoles. O-Phenanthiyl cupreidine and cupreine derivatives PHNO-CPD and PHNO-CPN were identified as optimal structures, allowing the use of aiyl and allgmyl pyruvates, glyoxalate and (electron-poor) benzaldehydes in this reaction (Scheme 14.18). ... 

Figure 6.1 Structures of the natural cinchona alkaloids and of cupreine and cupreidine. The analogs of quinine, quinidine, cinchonidine, and cinchonine with an ethyl at C3 (the dihydro species) are also isolated from natural sources.

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