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Long-range electron transfer in heme proteins.
Experimental work on heme proteins indicates that the electron-transfer rate falls off exponentially with donor-acceptor distance at long range, but the rate is greatly enhanced in proteins in which the structural changes accompanying electron transfer are very small.
Spectroelectrochemical study of the cytochrome a site in carbon monoxide inhibited cytochrome c oxidase.
The reduction potential of the Cytochrome a site in the carbon monoxide derivative of beef heart cytochrome c oxidase has been studied under a variety of conditions by thin-layer spectroelectrochemistry and the titration behavior of the site is consistent with a moderately strong anticooperative interaction between cy tochrome a and CuA.
Variable-temperature spectroelectrochemical study of horseradish peroxidase.
The results suggest that compound I is more reactive toward outer-sphere reductants than compound II, and the reorganization energy for the macrocycle-centered couple is lower than that for the metal-centered one.
Spectrochemical studies on the blue copper protein azurin from Alcaligenes denitrificans.
The distinctly lower Eo values for azurins, as compared with plastocyanins, are related to the more copper(II)-like site in azurin [with a weaker Cu-S(Met) interaction and a Cu-O interaction not found in plastOCyanin].
Is what you eat and drink safe? Detection and identification of microbial contamination in foods and water
A high-sensitivity, multiwavelength fluorescence detector and signal- collection and processing software that enables one to distinguish between abiotic matter, sporulated bacteria, vegetative bacteria, dead bacteria, and other biomaterials containing aromatic amino acids.
Real-time In-situ Detection of Microbes
A point of care disposable diagnostic based on the en masse capture of blood-borne microbes from 1 mL of fresh whole blood with surface-tethered, small molecule ligands that provides an estimate of the total microbial load as well as the relative distribution of live cells, dead cells, and endospores.
Temperature dependence of the reduction potential of CuA in carbon monoxide inhibited cytochrome c oxidase.
The temperature dependence of the reduction potential of the CuA site in carbon monoxide inhibited cytochrome c oxidase has been measured with a spectroelectrochemical method adapted to the