Cytochrome-C Bovine

Cytochrome-C Bovine, also known as bovine cytochrome c, is a small hemeprotein found in the mitochondria of bovine cells. It plays a crucial role in the electron transport chain, which is essential for cellular respiration and energy production. This protein is highly conserved across different species, making it a valuable model for studying various biological processes, including apoptosis and oxidative stress.

Cytochrome-C Bovine is composed of a single polypeptide chain with a molecular weight of approximately 12,000 daltons . The protein contains a heme group, which is responsible for its electron transfer capabilities. The heme group consists of a porphyrin ring coordinated with an iron atom that can undergo oxidation and reduction, allowing cytochrome c to transfer electrons between Complex III (Coenzyme Q – Cyt c reductase) and Complex IV (Cyt c oxidase) in the mitochondrial inner membrane .

In the electron transport chain, cytochrome c accepts electrons from the cytochrome c1 subunit of Complex III and transfers them to Complex IV . This transfer is a critical step in the production of ATP, the primary energy currency of the cell. The ability of cytochrome c to undergo reversible oxidation and reduction makes it an efficient electron carrier, facilitating the flow of electrons and the generation of a proton gradient across the mitochondrial membrane .

Cytochrome-C Bovine also plays a significant role in the process of apoptosis, or programmed cell death. During apoptosis, cytochrome c is released from the mitochondria into the cytosol, where it interacts with apoptotic protease activating factor-1 (Apaf-1) and procaspase-9 to form the apoptosome . This complex activates caspase-9, which in turn activates downstream caspases, leading to the execution of the apoptotic program . The release of cytochrome c from the mitochondria is a key regulatory step in apoptosis and is tightly controlled by various proteins, including members of the Bcl-2 family .

Cytochrome c is highly conserved across eukaryotic species, including plants, animals, fungi, and many unicellular organisms . This conservation indicates its fundamental role in cellular metabolism and its importance in evolutionary biology. The small size and high solubility of cytochrome c make it an ideal model for studying protein structure, function, and evolution .

Due to its well-characterized structure and function, Cytochrome-C Bovine is widely used in biochemical and biophysical research. It serves as a model system for studying electron transfer reactions, protein-protein interactions, and the mechanisms of apoptosis . Additionally, its role in oxidative stress and its involvement in various diseases, including neurodegenerative disorders and cancer, make it a valuable target for therapeutic research .