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Spectral and Redox Properties of a Recombinant Mouse Cytochrome b561 Protein Suggest Transmembrane Electron Transfer Function

Cytochrome b561 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 t...

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Autores principales: Bérczi, Alajos, Márton, Zsuzsanna, Laskay, Krisztina, Tóth, András, Rákhely, Gábor, Duzs, Ágnes, Sebők-Nagy, Krisztina, Páli, Tibor, Zimányi, László
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10005133/
https://www.ncbi.nlm.nih.gov/pubmed/36903505
http://dx.doi.org/10.3390/molecules28052261
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author Bérczi, Alajos
Márton, Zsuzsanna
Laskay, Krisztina
Tóth, András
Rákhely, Gábor
Duzs, Ágnes
Sebők-Nagy, Krisztina
Páli, Tibor
Zimányi, László
author_facet Bérczi, Alajos
Márton, Zsuzsanna
Laskay, Krisztina
Tóth, András
Rákhely, Gábor
Duzs, Ágnes
Sebők-Nagy, Krisztina
Páli, Tibor
Zimányi, László
author_sort Bérczi, Alajos
collection PubMed
description Cytochrome b561 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.
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spelling pubmed-100051332023-03-11 Spectral and Redox Properties of a Recombinant Mouse Cytochrome b561 Protein Suggest Transmembrane Electron Transfer Function Bérczi, Alajos Márton, Zsuzsanna Laskay, Krisztina Tóth, András Rákhely, Gábor Duzs, Ágnes Sebők-Nagy, Krisztina Páli, Tibor Zimányi, László Molecules Article Cytochrome b561 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. MDPI 2023-02-28 /pmc/articles/PMC10005133/ /pubmed/36903505 http://dx.doi.org/10.3390/molecules28052261 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Bérczi, Alajos
Márton, Zsuzsanna
Laskay, Krisztina
Tóth, András
Rákhely, Gábor
Duzs, Ágnes
Sebők-Nagy, Krisztina
Páli, Tibor
Zimányi, László
Spectral and Redox Properties of a Recombinant Mouse Cytochrome b561 Protein Suggest Transmembrane Electron Transfer Function
title Spectral and Redox Properties of a Recombinant Mouse Cytochrome b561 Protein Suggest Transmembrane Electron Transfer Function
title_full Spectral and Redox Properties of a Recombinant Mouse Cytochrome b561 Protein Suggest Transmembrane Electron Transfer Function
title_fullStr Spectral and Redox Properties of a Recombinant Mouse Cytochrome b561 Protein Suggest Transmembrane Electron Transfer Function
title_full_unstemmed Spectral and Redox Properties of a Recombinant Mouse Cytochrome b561 Protein Suggest Transmembrane Electron Transfer Function
title_short Spectral and Redox Properties of a Recombinant Mouse Cytochrome b561 Protein Suggest Transmembrane Electron Transfer Function
title_sort spectral and redox properties of a recombinant mouse cytochrome b561 protein suggest transmembrane electron transfer function
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10005133/
https://www.ncbi.nlm.nih.gov/pubmed/36903505
http://dx.doi.org/10.3390/molecules28052261
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