منابع مشابه
The mechanism of metmyoglobin oxidation.
The chemical behavior of metmyoglobin has received considerable attention, notably by Keilin and Hartree (1) and by George (2) and George and Irvine (3-5), on the grounds that it has the same prosthetic group as peroxidase and catalase and reacts with II&&, but at a rate more convenient for kinetic investigation. Although the mechanism of HzOz decomposition has proved t.o be different, this in ...
متن کاملOxidation - Reduction Potentials of the Metmyoglobin - Myoglobin System
The similarity in composition and function between myoglobin and hemoglobin has prompted numerous comparisons of the physicochemical properties of these two important biological pigments (8). Quantitative differences in their molecular weights (12, 14, 18), solubilities (9), absorption spectra (19), and equilibria with oxygen or carbon monoxide (6, 20) have been established. The presence in bot...
متن کاملA possible structure for the higher oxidation state of metmyoglobin.
In a previous paper (George & Irvine, 1954a) we concluded that there are two kinds of structure for the higher oxidation state of metmyoglobin (MetMb) which could explain the experimental observations. One is a radical structure formed by hydrogen atom removal from a methine carbon atom, a pyrrolic carbon atom or some other atom within the conjugated network of porphyrin ring and haemoprotein l...
متن کاملThe Gas Phase Oxidation of Acetaldehyde Reaction Mechanism and Kinetics
The mechanism of the low temperature oxidation of gaseous acetaldehyde was investigated in the temperature range of 1 50-400?°C. The minor, intermediate and major products were identified and measured quantitatively by sampling directly into the ionization chamber of an MS10-C2 mass spectrometer from the reactor. The formation of H2O, CO, CO2, HCOOH, H2, HCHO, CH3COOH and CH3OH as the major pro...
متن کاملMetmyoglobin Oxidation during Electron Transport Reactions in Mitochondria
Studies of the intracellular role of myoglobin were carried out by recording spectrophotometric changes in acid metmyoglobin and oxymyoglobin during electron transport reactions with mitochondria prepared from pigeon heart muscle by the method of Chance and Hagihara. The absorption peak of metmyoglobin at 409 mmicro disappeared when substrate was added to normal or antimycin-inhibited preparati...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1963
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)81216-9