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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 ...
There is no "cytochrome e," but cytochrome f, found in the cytochrome b 6 f complex of plants is a c-type cytochrome. [12] In mitochondria and chloroplasts, these cytochromes are often combined in electron transport and related metabolic pathways: [13]
The H subunit, shown in gold, lies on the cytoplasmic side of the plasma membrane. A cytochrome subunit, not shown here, contains four c-type hemes and is located on the periplasmic surface (outer) of the membrane. The latter sub-unit is not a general structural motif in photosynthetic bacteria.
The mobile water-soluble electron carrier is cytochrome c 6 in cyanobacteria, having been replaced by plastocyanin in plants. [8] Cyanobacteria can also synthesize ATP by oxidative phosphorylation, in the manner of other bacteria. The electron transport chain is NADH dehydrogenase → plastoquinol → b 6 f → cyt c 6 → cyt aa 3 → O 2
Photosynthetic reaction centre proteins are main protein components of photosynthetic reaction centres (RCs) of bacteria and plants. They are transmembrane proteins embedded in the chloroplast thylakoid or bacterial cell membrane. Plants, algae, and cyanobacteria have one type of PRC for each of its two photosystems.
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.
Cytochrome c is also found in some bacteria, where it is located within the periplasmic space. [ 9 ] Within the inner mitochondrial membrane, the lipid -soluble electron carrier coenzyme Q10 (Q) carries both electrons and protons by a redox cycle. [ 10 ]
In 1950, first experimental evidence for the existence of photophosphorylation in vivo was presented by Otto Kandler using intact Chlorella cells and interpreting his findings as light-dependent ATP formation. [1] In 1954, Daniel I. Arnon et.al. discovered photophosphorylation in vitro in isolated chloroplasts with the help of P 32. [2]