Copper and iron play important roles in a variety of biological processes, especially when being chelated with proteins. The proteins involved in the metal binding, transporting and metabolism have aroused much interest. To facilitate the study on this topic, we constructed two databases (DCCP and DICP) containing the known copper- and iron-chelating proteins, which are freely available from th...

As a result of the adaptation of life to an aerobic environment, nature has evolved a panoply of metalloproteins for oxidative metabolism and protection against reactive oxygen species. Despite the diverse structures and functions of these proteins, they share common mechanistic grounds. An open-shell transition metal like iron or copper is employed to interact with O2 and its derived intermedi...

We report a versatile infrared spectroscopic method for studying redox chemistry of metalloproteins, and demonstrate for the first time electrochemically-induced changes to the active site of the regulatory [NiFe]-hydrogenase from Ralstonia eutropha. A carbon particle network working electrode allows control over a wide potential window without the need for solution mediators.

Background: Metalloproteins are proteins capable of binding one or more metal ions, which may be required for their biological function, for regulation of their activities or for structural purposes. Metal-binding properties remain difficult to predict as well as to investigate experimentally at the whole-proteome level. Consequently, the current knowledge about metalloproteins is only partial....

Polarity Reversed-phase chromatography and hydrophobic-interaction chromatography Centrifugation: Analytical Centrifugation. Chromatography: Protein Separation. III/Enzymes: Liquid Chromatography. Proteins: Capillary Electrophoresis; Centrifugation; Crystallization; Electrophoresis; Glycoproteins: Liquid Chromatography; High-Speed Countercurrent Chromatography; Ion Exchange; Metalloproteins: Ch...

We report the use of triazacyclophane (TAC)-scaffolded amino acids as a structural mimic for 3-histidine metal-binding sites in metalloproteins, especially for the mimicry of type-3 copper binding sites as are present in hemocyanin, tyrosinase and catechol oxidase.

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De novo protein design has recently emerged as an attractive approach for studying the structure and function of proteins. This approach critically tests our understanding of the principles of protein folding; only in de novo design must one truly confront the issue of how to specify a protein's fold and function. If we truly understand proteins, it should be possible to design receptors, enzym...

E.p.r. is a spectroscopic technique that probes the environment of a paramagnetic centre by defining tlie size and shape of the magnetic moment produced by the unpaired electron. and by characterizing any magnetic fields which might be produced by the parent molecule in the vicinity of the paramagnetic centre. In the context of our interests, these unpaired electrons are found either in selecte...

This commentary outlines a protein engineering approach as an alternative to immobilisation developed in our laboratory. We use a recombinant silk protein into which metal active sites can be incorporated to produce solid-state metalloprotein materials. The silk protein directly coordinates to the metal centres providing control over their reactivity akin to that seen in naturally occurring met...