Approaches to electrochemical ET mechanisms of multi-centre metalloproteins

In the following, we proceed to several new aspects regarding molecular resolution of adsorbed metalloproteins. In Section 5.3, we first show that close to molecular resolution of the interfacial ET patterns of some two-centre proteins is within reach. The number of intermetallic interactions and resulting microscopic reduction potentials and rate constants in metalloproteins with more than two centres is, however, prohibitively large for such resolution. In Section 5.4 we address molecular and supramolecu-lar adsorption. We show here that in situ STM and AFM, indeed do hold exciting new perspectives for this important and central structural aspect of proteins at surfaces. 

We illustrate these aspects of metalloprotein dynamics at surfaces by two specific proteins. One is the two-centre bacterial di-heme protein cyt c4 from Pseudomonas stutzeri, and the other is the fungal four-centre redox enzyme laccase from Polyporus versicolor. 

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Approaches to electrochemical ET mechanisms of multi-centre metalloproteins 137... 

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