Cytochrome b5, its functions, structure and membrane topology.
The first part of the present communication reviews recent advances in our understanding of the known physiological functions of cytochrome b5. In addition, one section is devoted to a description of a recently discovered function of cytochrome b5, namely its involvement in the synthesis of the oncofetal antigen N-glycolylneuraminic acid. The second part of the article summarizes site-directed mutagenesis studies, primarily conducted in the author's laboratory, in both the catalytic heme-binding and membrane-binding domain of cytochrome b5. These studies have shown that: 1) the membrane binding domain of cytochrome b5 spans the bilayer; 2) cytochrome b5 lacking 19 COOH-terminal amino acids does not bind to membrane bilayers; and 3) specific amino acids in the membrane binding domain have been mutated and shown not to be essential for the function of cytochrome b5 with its redox partners.
Vergéres
G
G
Department of Biophysical Chemistry, University of Basel, Switzerland.
Waskell
L
L
D000595:Amino Acid Sequence; D000818:Animals; D015786:Cytochromes b5 / Q000737:chemistry / Q000502:physiology*; D006801:Humans; D008055:Lipids / Q000096:biosynthesis*; D008565:Membrane Proteins / Q000737:chemistry / Q000502:physiology*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D017434:Protein Structure, Tertiary; D013329:Structure-Activity Relationship
D008055:Lipids; D008565:Membrane Proteins; D015786:Cytochromes b5