Mitochondria is an organelle which is commonly found in large numbers in most cells, in which the biochemical processes of respiration and energy production occur. It has a double membrane, the inner layer being folded inward to form layers.
The term mitochondrion is coined by C. Benda. These are energy converting organelles, which are present in virtually all eukaryotic cells.
Structure of Mitochondria:
The mitochondria are covered with two membranes:
The outer membrane is fairly smooth. It has special proteins embedded into the membrane called porins which are intrinsic proteins responsible for the transport of molecules across the membrane. The outer membrane protects the organelle, and porins allow free passage for various molecules into the inner-mitochondrial space of the mitochondria.
Mitochondrial porins are voltage dependent anion-selective channels that allow the passage of small molecules across the mitochondrial outer membrane.
Inner membrane is highly convoluted; forming folds called cristae. The inner membrane is also very impermeable to many solutes due to the high content of a phospholipid called cardiolipin
. The cristae greatly increase the inner membrane’s surface area.
The two faces of this membrane are referred to as the matrix side and the cytosolic side. Inner membrane contains enzymes complex called ATP synthase (also called F0-
complex or oxysomes) that make ATP.
Hydrogenosome and mitosomes:
Some primitive protists such as Trichomonas vaginalis
lack mitochondria. These protists contain a specialized organelle, involved in synthesis of ATP abd hydrogen, called the hydrogenosome. These are the site of fermentative oxidation of pyruvate, coupled with ATP production via substrate level phosphorylation.
Like mitochondria, hydrogenosome are surrounded by a double membrane and produce ATP. In contrast to mitochondria, hydrogenosomes produce molecules hydrogen through fermentations, lack cytochromes and usually lack DNA.
, organelles of mitochondrial origin, are double membrane bound organelles found in some unicellular eukaryotes, including Entamoeba histolytica
and microsporidia. The mitosome has been detected only in anaerobic organisms that do not have mitochondria.
Functions of mitochondria:
Mitochondria has an important function is to harvest energy. The simpler compounds obtained from nutrition are carried to the mitochondria where they are further processed and converted to charged molecules. These charged molecules again chain with oxygen and produce ATP molecules. This process is referred as oxidative phosphorylation.
Mitochondria aid the cells to sustain proper concentration of calcium ions within the partitions of the cell.
The mitochondria also supports in building certain fragments of blood and hormones like testosterone and estrogen.
The mitochondria in liver cells have enzymes for detoxifying ammonia.
The mitochondria also play an important role apoptosis (also called as programmed cell death). Irregular death of cells due to the deformity in mitochondria can affect the function of organ.
Targeting of mitochondrial proteins:
Mitochondrial proteins are synthesized by cytosolic as well as matrix ribosomes. About 99% of mitochondrial proteins are encoded by nuclear genes and are synthesized as precursors on cytosolic ribosomes. Proteins synthesized by cytosolic ribosomes are translocated into mitochondria post- translationally. Proteins imported into mitochondria may be located into outer membrane, the intermembrane space, the inner membrane or the matrix.
Mitochondrial protein import requires membrane receptors and translocons. Import is initiated by the binding of a mitochondrial targeting sequence to an import receptor in the outer mitochondrial membrane. Two distinct translocation complexes that mediate translocation are situated in the outer and inner mitochondrial membranes, referred to as TOM (Translocase of the outer membrane) complex and TIM (Translocase of inner membrane) complex.
Both translocases have to cooperate tightly to promote protein translocation. The TOM complex consists of seven different subunits. The receptors Tom20, Tom22, Tom70 recognize precursor proteins and transfer them to the central component, the channel forming Tom40. Three small Tom proteins Tom5, Tom6, and Tom7, are tangled in the association and dynamics of the TOM complex.