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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 08 Dec 2016.

Cytochrome b5 type A

cytochrome b5
a heme protein that may act as an electron transporter [RGD, Feb 2006] (from NCBI)
Papers on cytochrome b5
Nitric-oxide dioxygenase function of human cytoglobin with cellular reductants and in rat hepatocytes.
GeneRIF
Gardner et al., Cincinnati, United States. In J Biol Chem, 2010
Cygb has a nitric-oxide dioxygenase function and ascorbate and cytochrome b(5) have roles as reductants
Electron transfer properties and catalytic competence of cytochrome b5 in the fusion protein Hmwb5-EGFP in reactions catalyzed by cytochrome P450 3A4.
GeneRIF
Usanov et al., Minsk, Belarus. In Biochemistry (mosc), 2009
The hydrophobic domain of cytochrome b5 participates not only in hemeprotein interaction, but also in electron transfer from cytochrome b5 to cytochrome P4503A4.
Structural propensities in the heme binding region of apocytochrome b5. I. Free peptides.
GeneRIF
Lecomte et al., United States. In Biopolymers, 2007
The data distinguished the four helical segments and provided insight into the existence of holo- and nonholo-like interactions in the cytochrome's heme binding site.
Structural propensities in the heme binding region of apocytochrome b5. II. Heme conjugates.
GeneRIF
Lecomte et al., United States. In Biopolymers, 2007
The effect of the His63-iron bond and proximity of heme plane on the population of helical conformation in H4 and H5 of cytochrome b5 was investigated.
Influence of point mutations on the flexibility of cytochrome b5: molecular dynamics simulations of holoproteins.
GeneRIF
Kuczera et al., Lawrence, United States. In Biopolymers, 2006
simulations provided qualitative microscopic explanations of many of the differences in physical properties between outer mitochondrial membrane CYB5 isoform and microsomal CYB5 and two mutants in terms of localized changes in structure and flexibility
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