(બાયોકેમિસ્ટ્રી,

cytochromes's Usage Examples:

number of other biologically important hemoproteins such as myoglobin, cytochromes, catalases, heme peroxidase, and endothelial nitric oxide synthase.

an [2Fe-2S] iron–sulfur cluster and three cytochromes: one cytochrome c1 and two b cytochromes.

Biochemistry and Molecular Biology (IUBMB), cytochromes a, cytochromes b, cytochromes c and cytochrome d.

Within the second helix is the sequence motif for the c-type cytochromes, CxxCH (residues 21–25), which is covalently attached to the haem through.

Cristae are studded with proteins, including ATP synthase and a variety of cytochromes.

The differences between those cytochromes lies in the different side-chains.

oxygen sensors and the haem-containing cytochromes that undergo reversible one-electron reduction during oxidative-phosphorylation.

For example, vertebrate cytochromes c all have dipole moment of approximately.

"Microbial cytochromes P450: biodiversity and biotechnology.

Cytochrome c is highly water-soluble, unlike other cytochromes, and is an essential component of the electron transport chain, where.

"Identification of constitutive and herbicide inducible cytochromes P-450 in Streptomyces griseolus".

Types of well-studied cytochromes include cytochromes a-c, cytochrome oxidase, and cytochrome P450.

Cytochromes c (cyt c, c-type cytochromes) cytochromes, or heme-containing proteins, that have heme C covalently attached to the peptide backbone via one.