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Cytochrome c is a highly conserved protein across the spectrum of eukaryotic species, found in plants, animals, fungi, and many unicellular organisms. This, along with its small size (molecular weight about 12,000 daltons), [7] makes it useful in studies of cladistics. [8] Cytochrome c has been studied for the glimpse it gives into evolutionary ...
Since these systems do not work by exchanging ions, like traditional water softeners do, one benefit claimed for the user is the elimination of the need to add salt to the system. Such systems do not remove minerals from the water itself. Rather, they can only alter the downstream effects that the mineral-bearing water would otherwise have.
Complex III itself is composed of several subunits, one of which is a b-type cytochrome while another one is a c-type cytochrome. Both domains are involved in electron transfer within the complex. Complex IV contains a cytochrome a/a3-domain that transfers electrons and catalyzes the reaction of oxygen to water.
Q-cytochrome c oxidoreductase is also known as cytochrome c reductase, cytochrome bc 1 complex, or simply complex III. [35] [36] In mammals, this enzyme is a dimer, with each subunit complex containing 11 protein subunits, an [2Fe-2S] iron–sulfur cluster and three cytochromes: one cytochrome c 1 and two b cytochromes. [37]
The ultimate products of the Q cycle are four protons entering the intermembrane space, two from the matrix and two from the reduction of two molecules of cytochrome c. The reduced cytochrome c is eventually reoxidized by complex IV. The process is cyclic as the ubiquinol created at the Q i site can be reused by binding to the Q o site of ...
Small soluble cytochrome c proteins with a molecular weight of 8-12 kDa and a single heme group belong to class I. [10] [11] It includes the low-spin soluble cytC of mitochondria and bacteria, with the heme-attachment site located towards the N-terminus, and the sixth ligand provided by a methionine residue about 40 residues further on towards the C-terminus.
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