Spectral and Redox Properties of a Recombinant Mouse Cytochrome b 561 Protein Suggest Transmembrane Electron Transfer Function.
Alajos BércziZsuzsanna MártonKrisztina LaskayAndrás TóthGábor RakhelyÁgnes DuzsKrisztina Sebők-NagyTibor PáliLászló ZimányiPublished in: Molecules (Basel, Switzerland) (2023)
Cytochrome b 561 proteins (CYB561s) are integral membrane proteins with six trans-membrane domains, two heme- b redox centers, one on each side of the host membrane. The major characteristics of these proteins are their ascorbate reducibility and trans-membrane electron transferring capability. More than one CYB561 can be found in a wide range of animal and plant phyla and they are localized in membranes different from the membranes participating in bioenergization. Two homologous proteins, both in humans and rodents, are thought to participate-via yet unidentified way-in cancer pathology. The recombinant forms of the human tumor suppressor 101F6 protein (Hs_CYB561D2) and its mouse ortholog (Mm_CYB561D2) have already been studied in some detail. However, nothing has yet been published about the physical-chemical properties of their homologues (Hs_CYB561D1 in humans and Mm_CYB561D1 in mice). In this paper we present optical, redox and structural properties of the recombinant Mm_CYB561D1, obtained based on various spectroscopic methods and homology modeling. The results are discussed in comparison to similar properties of the other members of the CYB561 protein family.
Keyphrases
- electron transfer
- protein protein
- endothelial cells
- amino acid
- mental health
- randomized controlled trial
- cell free
- binding protein
- physical activity
- type diabetes
- systematic review
- small molecule
- molecular docking
- magnetic resonance
- skeletal muscle
- oxidative stress
- optical coherence tomography
- high speed
- lymph node metastasis
- meta analyses
- cell wall
- wild type
- contrast enhanced
- childhood cancer