Reduction–oxidation (redox) reactions provide a distinct modality for biological communication that is fundamentally different from the more-familiar ion-based electrical modality. Biology uses these two modalities through systems (immune versus nervous), and mechanisms to control flow of charge carriers: soluble ions controlled using structural barriers (i.e., membranes) gates (e.g., membrane-...

The work exploring the stoichiometry of Pt deposition via surface-limited redox replacement of the underpotentially deposited UPD Cu monolayer on Au 111 is presented. The Cu UPD monolayer is formed from 10−3 M Cu2+ + 0.1 M HClO4 solution, whereas the Pt deposition via surface-limited redox replacement reaction is carried out in 10−3 M PtCl6 2− + 0.1 M HClO4 solution at open-circuit potential. O...

Because of their cell surface locations, the outer membrane c-type cytochromes MtrC and OmcA of Shewanella oneidensis MR-1 have been suggested to be the terminal reductases for a range of redox-reactive metals that form poorly soluble solids or that do not readily cross the outer membrane. In this work, we determined the kinetics of reduction of a series of Fe(III) complexes with citrate, nitri...

In general, hemoproteins are capable of catalyzing redox reactions. Aldoxime dehydratase (OxdA), which is a unique heme-containing enzyme, catalyzes the dehydration of aldoximes to the corresponding nitriles. Its reaction is a rare example of heme directly activating an organic substrate, unlike the utilization of H2O2 or O2 as a mediator of catalysis by other heme-containing enzymes. While it ...

The befitting capping capabilities of AsO4(3-) provide a stable Cu2O nanocatalyst from a galvanic reaction between a Cu(II) precursor salt and As(0) nanoparticles. This stable Cu2O hydrosol appears to be a suitable catalyst for the one-electron transfer reversible redox reaction between Eosin Y and NaBH4. The progress of the reaction relates to three different kinetic stages. In the presence of...

Photosystem II, the photosynthetic water-oxidizing complex, contains two redox-active tyrosine residues. Although current models suggest that these tyrosines are located in symmetric positions in the reaction center, there are functional differences between them. To elucidate those structural factors that give rise to this functional asymmetry, we have used difference Fourier-transform infrared...

Photoinduced electron transfer in biological systems, especially in proteins, is a highly intriguing matter. Its mechanistic details cannot be addressed by structural data obtained by crystallography alone because this provides only static information on a given redox system. In combination with transient spectroscopy and site-directed manipulation of the protein, however, a dynamic molecular p...