Filtry
Preparation of apo-cytochrome b5 utilizing heme transfer to apo-myoglobin
To prepare apo-cytochrome b5, heme transfer from native cytochrome b5 to a protein with higher affinity toward the heme, the horse heart apo-myoglobin, was utilized....
CE - Biochemie
- 2009 •
- Jx
Rok uplatnění
Jx - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)
"Vinyl connection" - another mechanism of heme-apoprotein communication?
The obtained data show the possible role of the vinyl side-chains of the heme in cytochrome P450 in the heme-apoprotein information transfer. From the viewpoint of vinyl mobility the P450 forms may be grouped into three cla...
CE - Biochemie
- 2011 •
- D
Rok uplatnění
D - Stať ve sborníku
Heme: Emergent roles of heme in signal transduction, functional regulation and as catalytic centres
Protoporphyrin IX iron complex (heme) is an important cofactor for oxygen transfer, oxygen storage, oxygen activation, and electron transfer when bound to the heme proteins hemoglobin, myoglobin, cytochrome P450 an...
Biochemistry and molecular biology
- 2019 •
- Jimp •
- Odkaz
Rok uplatnění
Jimp - Článek v periodiku v databázi Web of Science
Výsledek na webu
Gaseous O-2, NO, and CO in Signal Transduction: Structure and Function Relationships of Heme-Based Gas Sensors and Heme-Redox Sensors
for peroxidase; and the electron transfer site for cytochromes.1MINUS SIGN 8 The heme iron are transferred to/from the partner protein via the heme iron complex, whereas for peroxThe heme iron complex is ...
CE - Biochemie
- 2015 •
- Jx •
- Odkaz
Rok uplatnění
Jx - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)
Výsledek na webu
Do multiheme cytochromes containing close-packed heme groups have a band structure formed from the heme π and π* orbitals?
Multiheme cytochromes (MHCs) are bacterial electron-transfer proteins. We show contain occupied and unoccupied bands formed from heme Tc and Tc* orbitals that span hemes are electronically coupled according to EPR data and ...
Physical chemistry
- 2024 •
- Jimp •
- Odkaz
Rok uplatnění
Jimp - Článek v periodiku v databázi Web of Science
Výsledek na webu
Heme pathway evolution in kinetoplastid protists
, and that lateral gene transfer has played a role in the evolution of heme biosynthesis, the heme pathway-a core metabolic pathway in a wide range of organisms-is incomplete for heme biosynthesis by acquiring ...
EB - Genetika a molekulární biologie
- 2016 •
- Jx •
- Odkaz
Rok uplatnění
Jx - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)
Výsledek na webu
Make It, Take It, or Leave It: Heme Metabolism of Parasites
Heme and other tetrapyrroles, often called ?the colors of life, belong]. The major product of tetrapyrrole biosynthesis in non-photosynthetic organisms is heme, an iron-coordinated porphyrin with the capacity to transfer el...
EB - Genetika a molekulární biologie
- 2013 •
- Jx •
- Odkaz
Rok uplatnění
Jx - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)
Výsledek na webu
Signal transduction mechanisms in heme-based globin-coupled oxygen sensors with a focus on a histidine kinase (AfGcHK) and a diguanylate cyclase (YddV or EcDosC)
Heme is a vital cofactor of proteins with roles in oxygen transport (e.g transfer (e.g. cytochromes) and many other functions. However, its structural discusses the mechanism of signal transduction in two heme-based oxygen ...
Biochemistry and molecular biology
- 2022 •
- Jimp •
- Odkaz
Rok uplatnění
Jimp - Článek v periodiku v databázi Web of Science
Výsledek na webu
Holoenzyme structures of endothelial nitric oxide synthase - An allosteric role for calmodulin in pivoting the FMN domain for electron transfer
the cross-electron transfer from the reductase in one monomer to the heme in theopposite monomer. The heme domain acts as the anchoring dimeric structure for the entire enzymeWhile the three-dimensional structures of h...
CE - Biochemie
- 2014 •
- Jx •
- Odkaz
Rok uplatnění
Jx - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)
Výsledek na webu
Kinetics and Energetics of Intramolecular Electron Transfer in Single-Point Labeled TUPS-Cytochrome c Derivatives
Electron transfer within and between proteins is a fundamental biological as an electron donor to the oxidized heme c. The rates of the forward (from the label to the heme) and the reverse (from the reduced heme ba...
Physical chemistry
- 2021 •
- Jimp •
- Odkaz
Rok uplatnění
Jimp - Článek v periodiku v databázi Web of Science
Výsledek na webu
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