Oxidation of deoxy myoglobin by [Fe(CN)6]3-.

The ability of myoglobin (Mb) to reversibly bind O2 and other ligands has been well characterized. Mb also participates with a variety of redox metals to form metmyoglobin (metMb). By using an anaerobic stopped-flow device we have measured outer-sphere oxidation by [Fe(CN)6]3 of native sperm whale myoglobin, recombinant wild-type Mb, and a series of mutant Mb proteins in which the distal His-64 was changed to Gly, Phe, Leu or Val.

Neuroelectric assessment of nutrient intake.

Electroencephalographic (EEG) activity and auditory event-related brain potentials (ERPs) were assessed in two groups (n = 12 each) of subjects. The 'food-nutrient' group had fasted from the night before and consumed a 500 cal nutrient drink; the 'control' group consumed breakfast but did not consume any nutrients during the recordings. All subjects were assessed every 15 min for six trial blocks at the same time of day, with the fast/nutrient group measured initially before and after consuming the nutrient drink.

Copper-specific damage in human erythrocytes exposed to oxidative stress.

Ascorbate and complexes of Cu(II) and Fe(III) are capable of generating significant levels of oxygen free radicals. Exposure of erythrocytes to such oxidative stress leads to increased levels of methemoglobin and extensive changes in cell morphology. Cu(II) per mole is much more effective than Fe(III).

Hemoglobin: a mechanism for the generation of hydroxyl radicals.

Oxyhemoglobin (HbO2) reduces Fe(III)NTA aerobically to become methemoglobin (metHb) and Fe(II)NTA. These conditions are favorable for the generation via Fenton chemistry of the hydroxyl radical that was measured by HPLC using salicylate as a probe. The levels of hydroxyl radicals generated are a function of both the percent metHb formed and the chemical nature of the buffer.