It can be found within the cellular mitochondrial matrix.

This enyzme is present the mitochondrial matrix of fungi and mammals.

For example, the mitochondrial matrix separates the mitochondrion into compartments.

The protein is located in the mitochondrial matrix.

During this process, four protons are translocated from the mitochondrial matrix to the intermembrane space.

Also acts in mitochondrial matrix as molecular chaperone.

Once inside the mitochondrial matrix, fatty acids undergo β-oxidation.

It is synthesized using cytoplasmic ribosomes, then transported into the mitochondrial matrix.

Pyruvate dehydrogenase complex is located in the mitochondrial matrix of eukaryotes.

Once the fatty acid is inside the mitochondrial matrix, Beta Oxidation can begin.

Once activated, the acyl CoA is transported into the mitochondrial matrix.

Unlike most mitochondrial matrix proteins, it contains a non-cleavable amino-terminal targeting signal.

In the eukaryotes the majority of the Lon proteases are located in the mitochondrial matrix.

Mitochondrial matrix targeting sequences are rich in positively charged amino acids and hydroxylated ones.

The mitochondrial matrix also contains the mitochondria's DNA and ribosomes.

Cpt2 transfers carnitinoyl residues to CoA in the mitochondrial matrix for β-oxidation.

Several of the enzymes in the cycle may be loosely associated in a multienzyme protein complex within the mitochondrial matrix.

The TIM23 complex facilitates translocation of matrix-targeted proteins into the mitochondrial matrix.

The lipophilic cation used is based on the triphenylphosphonium structure, which is well known to accumulate within the negative mitochondrial matrix.

The mitochondrial matrix protein p32 stabilizes smARF.

In mammals this enzyme participates in the urea cycle and is located in the mitochondrial matrix.

Under certain conditions, protons can re-enter the mitochondrial matrix without contributing to ATP synthesis.

In yeast, the Lon protease PIM1 is located in the mitochondrial matrix.

It encodes a mitochondrial matrix protein that forms a homotetramer and binds one manganese ion per subunit.

In mitochondria, energy released by the electron transport chain is used to move protons from the mitochondrial matrix to the intermembrane space of the mitochondrion.