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American Chemical Society, Accounts of Chemical Research, 1(47), p. 56-65, 2013

DOI: 10.1021/ar4000696

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Unveiling the Details of Electron Transfer in Multicenter Redox Proteins

Journal article published in 2013 by Catarina M. Paquete ORCID, Ricardo O. Louro ORCID
This paper was not found in any repository, but could be made available legally by the author.
This paper was not found in any repository, but could be made available legally by the author.

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Abstract

Metalloproteins modulate the intrinsic properties of transition metals to achieve controlled catalysis, electron transfer, or structural stabilization. Those performing electron transport, redox proteins, are a diverse class of proteins with central roles in numerous metabolic and signaling pathways, including respiration and photosynthesis. Many redox proteins have applications in industry, especially biotechnology, making them the focus of intense research. Redox proteins may contain one or multiple redox centers of the same or a different type. The complexity of proteins with multiple redox centers makes it difficult to establish a detailed molecular mechanism for their activity. Thermodynamic and kinetic information can be interpreted using the molecular structure to elucidate the protein’s functional mechanism.