Macrocyclic Metal Complexes for Metalloenzyme Mimicry and Sensor Development

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• 作者：Tanmaya Joshi ; Bim Graham ; Leone Spiccia
• 刊名：Accounts of Chemical Research
• 出版年：2015
• 出版时间：August 18, 2015
• 年：2015
• 卷：48
• 期：8
• 页码：2366-2379
• 全文大小：846K
• ISSN：1520-4898

文摘

Examples of proteins that incorporate one or more metal ions within their structure are found within a broad range of classes, including oxidases, oxidoreductases, reductases, proteases, proton transport proteins, electron transfer/transport proteins, storage proteins, lyases, rusticyanins, metallochaperones, sporulation proteins, hydrolases, endopeptidases, luminescent proteins, iron transport proteins, oxygen storage/transport proteins, calcium binding proteins, and monooxygenases. The metal coordination environment therein is often generated from residues inherent to the protein, small exogenous molecules (e.g., aqua ligands) and/or macrocyclic porphyrin units found, for example, in hemoglobin, myoglobin, cytochrome C, cytochrome C oxidase, and vitamin B₁₂. Thus, there continues to be considerable interest in employing macrocyclic metal complexes to construct low-molecular weight models for metallobiosites that mirror essential features of the coordination environment of a bound metal ion without inclusion of the surrounding protein framework.