cytochrome

This means that cytochrome c does not receive them.

For example, it occurs in human growth hormone and several varieties of cytochrome.

The founding member of this family is mitochondrial cytochrome c.

Its main function is to oxidise the Cytochrome c protein.

The cytochrome bc1 complex: function in the context of structure.

It belongs to the cytochrome c family of proteins.

The third, a d-type cytochrome is expressed only when the cells are grown under high pressure.

However, some current research is focused on the potential benefits of cytochrome P450 inhibition.

Three types of cytochrome are distinguished by their prosthetic groups:

Cytochrome c is also involved in initiation of apoptosis.

Another type of analysis on the cytochrome b sequence data produces the same result as morphology.

One thing to keep in mind is the fact that low blood sugar activates the cytochrome p450 system.

There is evidence that it induces cytochrome P-450 enzymes.

Cytochrome c, a protein of the mitochondrial electron transport chain.

The active site of cytochrome P450 contains a heme iron center.

The breast cancer treatment drug tamoxifen is also metabolized to its active state by the same cytochrome.

The definition of cytochrome c is not defined in terms of the heme group.

The cytochrome c molecule has been studied for the glimpse it gives into evolutionary biology.

There is no metabolic involvement of the hepatic cytochrome P450 system.

The sequences of the cytochrome b gene differ by about 10% in these two species.

A cytochrome is a kind of electron-transferring protein that contains at least one heme group.

This genes code for cytochrome P450s involved in fatty acid synthesis.

In fact, the cytochrome a and Cu form a binuclear center that is the site of oxygen reduction.

The reduced iron-sulfur center transfers its electron through cytochrome f to Pc.

Changes in other hepatic cytochrome p450 genes are included in Table 2.