منابع مشابه
Interaction of myoglobin and cytochrome C.
Spectrophotometric studies of various mixtures of reduced and oxidized forms of myoglobin and cytochrome c revealed that oxymyoglobin is capable of reducing ferricytochrome c at a molar ratio of 1. Other combinations, i.e. oxymyoglobin and ferrocytochrome c; metmyoglobin and ferricytochrome c; or metmyoglobin and ferrocytochrome c showed no spectral change during the time course studied. The pH...
متن کاملInteraction of Myoglobin and Cytochrome c*
Spectrophotometric studies of various mixtures of reduced and oxidized forms of myoglobin and cytochrome c revealed that oxymyoglobin is capable of reducing ferricytochrome c at a molar ratio of 1. Other combinations, i.e. oxymyoglobin and ferrocytochrome c; metmyoglobin and ferricytochrome c; or metmyoglobin and ferrocytochrome c showed no spectral change during the time course studied. The pH...
متن کاملFunctional analogues of cytochrome c oxidase, myoglobin, and hemoglobin.
The majority of modern organisms, including many prokaryotes, are aerobes;1 that is, they use molecular oxygen as the terminal electron acceptor for energy generation. Although nearly every redox gradient in nature appears to be utilized by one organism or another,2-4 aerobic metabolism predominates, in large part due to the highly exergonic nature of the four-electron, four-proton (4e/4H+) red...
متن کاملMechanism of peroxynitrite interaction with cytochrome c.
Kinetics of the reaction of peroxynitrite with ferric cytochrome c in the absence and presence of bicarbonate was studied. It was found that the heme iron in ferric cytochrome c does not react directly with peroxynitrite. The rates of the absorbance changes in the Soret region of cytochrome c spectrum caused by peroxynitrite or peroxynitrite/bicarbonate were the same as the rate of spontaneous ...
متن کاملSpectroscopic analysis of myoglobin and cytochrome c dynamics in isolated cardiomyocytes during hypoxia and reoxygenation.
Raman microspectroscopy was applied to monitor the intracellular redox state of myoglobin and cytochrome c from isolated adult rat cardiomyocytes during hypoxia and reoxygenation. The nitrite reductase activity of myoglobin leads to the production of nitric oxide in cells under hypoxic conditions, which is linked to the inhibition of mitochondrial respiration. In this work, the subsequent reoxy...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1972
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)45555-5