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Cytochrome b5 type A

cytochrome b5
a heme protein that may act as an electron transporter [RGD, Feb 2006] (from NCBI)
Top mentioned proteins: ACID, CAN, HAD, V1a, oxidoreductase
Papers on cytochrome b5
Membrane topology and search for potential redox partners of colon cancer specific cytochrome P450 2W1.
Ingelman-Sundberg et al., Stockholm, Sweden. In Febs Lett, Feb 2016
In contrast to other endoplasmic reticulum P450s we found completely inverted ER membrane topology of CYP2W1 using different approaches (redox sensitive luciferase assay and protease protection assay) and demonstrated that canonical CYP reductants, cytochrome P450 reductase and cytochrome b5 cannot serve as electron donors for CYP2W1.
Cytochrome P450 17A1 Interactions with the FMN Domain of its Reductase as Characterized by NMR.
Scott et al., United States. In J Biol Chem, Jan 2016
Although some human microsomal P450 enzymes can instead accept the second electron from cytochrome b5, for human steroidogenic CYP17A1, the CPR FMN domain delivers both electrons and b5 is an allosteric modulator.
Cytochrome b5 reductase 1 triggers serial reactions that lead to iron uptake in plants.
Hwang et al., South Korea. In Mol Plant, Jan 2016
Here, we present evidence that cytochrome b5 reductase 1 (CBR1) increases unsaturated fatty acid levels, which stimulates PM H(+)-ATPase activity and thereby leads to rhizosphere acidification.
Cytochrome b5 reductase, a plasma membrane redox enzyme, protects neuronal cells against metabolic and oxidative stress through maintaining redox state and bioenergetics.
Lee et al., Seoul, South Korea. In Age (dordr), Dec 2015
In this study, in order to investigate how cytochrome b5 reductase (b5R), one of the PM redox enzymes, regulates cellular response under stressed conditions, human neuroblastoma cells transfected with b5R were used for viability and mitochondrial functional assays.
Heme proteins of Giardia intestinalis.
Dayer et al., Peterborough, Canada. In Exp Parasitol, Dec 2015
This includes the protozoan parasite Giardia intestinalis, which encodes five known heme proteins: a flavohemoglobin and four members of the cytochrome b5 family.
Ferrous and ferric state of cytochromes P450 in intact Escherichia coli cells: a possible role of cytochrome P450-flavodoxin interactions.
Martinek et al., Praha, Czech Republic. In Neuro Endocrinol Lett, Nov 2015
Their activity is dependent on the presence of a suitable electron donor (eukaryotic NADPH:CYP oxidoreductase or cytochrome b5).
Electron Transfer Pathways in Cholesterol Synthesis.
Porter, Lexington, United States. In Lipids, Oct 2015
The electron-donor proteins for these enzymes include cytochrome P450 reductase and the cytochrome b5 pathway.
X-ray structure of a mammalian stearoyl-CoA desaturase.
Zhou et al., Houston, United States. In Nature, Sep 2015
The reaction requires molecular oxygen, which is activated by a di-iron centre, and cytochrome b5, which regenerates the di-iron centre.
The mammalian molybdenum enzymes of mARC.
Clement et al., Kiel, Germany. In J Biol Inorg Chem, Mar 2015
In the presence of NADH, mARC proteins exert N-reductive activity together with the two electron transport proteins cytochrome b5 type B and NADH cytochrome b5 reductase.
The anticancer drug ellipticine activated with cytochrome P450 mediates DNA damage determining its pharmacological efficiencies: studies with rats, Hepatic Cytochrome P450 Reductase Null (HRN™) mice and pure enzymes.
Frei et al., Praha, Czech Republic. In Int J Mol Sci, 2014
The finding showing that cytochrome b5 alters the ratio of ellipticine metabolites generated by CYP1A1/2 and 3A4 explained this paradox.
Endothelial cell expression of haemoglobin α regulates nitric oxide signalling.
Isakson et al., Charlottesville, United States. In Nature, 2012
Mechanistically, endothelial Hb α haem iron in the Fe(3+) state permits NO signalling, and this signalling is shut off when Hb α is reduced to the Fe(2+) state by endothelial cytochrome b5 reductase 3 (CYB5R3, also known as diaphorase 1).
Nitric-oxide dioxygenase function of human cytoglobin with cellular reductants and in rat hepatocytes.
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.
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.
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.
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.
Dap1/PGRMC1 binds and regulates cytochrome P450 enzymes.
Espenshade et al., Baltimore, United States. In Cell Metab, 2007
Despite the numerous physiological processes that P450 enzymes impact, the electron donors P450 oxidoreductase and cytochrome b5 are the only proteins known to interact with and modulate the activity of ER microsomal P450s.
Influence of point mutations on the flexibility of cytochrome b5: molecular dynamics simulations of holoproteins.
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
Genetic basis for the lack of N-glycolylneuraminic acid expression in human tissues and its implication to human evolution.
Suzuki, Saitama, Japan. In Proc Jpn Acad Ser B Phys Biol Sci, 2006
The hydroxylation was carried out by a complex formed with hydroxylase, cytochrome b5, and NADH-cytochrome b5 reductase.
Cytochrome P-450 3A4: regulation and role in drug metabolism.
Guengerich, Nashville, United States. In Annu Rev Pharmacol Toxicol, 1998
Several issues remain to be resolved regarding the catalytic activity of the P-450 3A4 protein, including rate-limiting steps and the need for cytochrome b5, divalent cations, and acidic phospholipid systems for optimal activity.
Incomplete arrest in the outer membrane sorts NADH-cytochrome b5 reductase to two different submitochondrial compartments.
Schatz et al., Basel, Switzerland. In Cell, 1995
The S. cerevisiae gene MCR1 encodes two mitochondrial isoforms of NADH-cytochrome b5 reductase.
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