@article{MTMT:33687467,
	title = {Spectral and Redox Properties of a Recombinant Mouse Cytochrome b561 Protein Suggest Transmembrane Electron Transfer Function},
	url = {https://m2.mtmt.hu/api/publication/33687467},
	author = {Bérczi, Alajos and Márton, Zsuzsanna and Laskay, Krisztina and Tóth, András and Rákhely, Gábor and Duzs, Ágnes and Sebőkné Nagy, Krisztina and Páli, Tibor and Zimányi, László},
	doi = {10.3390/molecules28052261},
	journal-iso = {MOLECULES},
	journal = {MOLECULES},
	volume = {28},
	unique-id = {33687467},
	issn = {1420-3049},
	abstract = {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.},
	year = {2023},
	eissn = {1420-3049},
	orcid-numbers = {Rákhely, Gábor/0000-0003-2557-3641; Páli, Tibor/0000-0003-1649-1097; Zimányi, László/0000-0002-5101-2023}
}

@article{MTMT:33181371,
	title = {Quinone binding site in a type VI sulfide:quinone oxidoreductase},
	url = {https://m2.mtmt.hu/api/publication/33181371},
	author = {Miklovics, Nikolett and Duzs, Ágnes and Balogh, Fanni and Paragi, Gábor and Rákhely, Gábor and Tóth, András},
	doi = {10.1007/s00253-022-12202-8},
	journal-iso = {APPL MICROBIOL BIOT},
	journal = {APPLIED MICROBIOLOGY AND BIOTECHNOLOGY},
	volume = {106},
	unique-id = {33181371},
	issn = {0175-7598},
	abstract = {Monotopic membrane-bound flavoproteins, sulfide:quinone oxidoreductases (SQRs), have a variety of physiological functions, including sulfide detoxification. SQR enzymes are classified into six groups. SQRs use the flavin adenine dinucleotide (FAD) cofactor to transfer electrons from sulfide to quinone. A type VI SQR of the photosynthetic purple sulfur bacterium, Thiocapsa roseopersicina (TrSqrF), has been previously characterized, and the mechanism of sulfide oxidation has been proposed. This paper reports the characterization of quinone binding site (QBS) of TrSqrF composed of conserved aromatic and apolar amino acids. Val331, Ile333, and Phe366 were identified near the benzoquinone ring of enzyme-bound decylubiquinone (dUQ) using the TrSqrF homology model. In silico analysis revealed that Val331 and Ile333 alternately connected with the quinone head group via hydrogen bonds, and Phe366 and Trp369 bound the quinones via hydrophobic interactions. TrSqrF variants containing alanine (V331A, I333A, F366A) and aromatic amino acid (V331F, I333F, F366Y), as well as a C-terminal alpha-helix deletion (CTD) mutant were generated. These amino acids are critical for quinone binding and, thus, catalysis. Spectroscopic analyses proved that all mutants contained FAD. I333F replacement resulted in the lack of the charge transfer complex. In summary, the interactions described above maintain the quinone molecule's head in an optimal position for direct electron transfer from FAD. Surprisingly, the CTD mutant retained a relatively high level of specific activity while remaining membrane-anchored. This is a unique study because it focuses on the QBS and the oxidative stage of a type VI sulfide-dependent quinone reduction.},
	keywords = {Sulfur metabolism; Disulfide reductase; Quinone reduction; Sulfide: quinone oxidoreductase (SQR); Quinone binding site},
	year = {2022},
	eissn = {1432-0614},
	pages = {7505-7517},
	orcid-numbers = {Paragi, Gábor/0000-0001-5408-1748; Rákhely, Gábor/0000-0003-2557-3641}
}

@article{MTMT:31719460,
	title = {Insights into the catalytic mechanism of type VI sulfide:quinone oxidoreductases},
	url = {https://m2.mtmt.hu/api/publication/31719460},
	author = {Duzs, Ágnes and Miklovics, Nikolett and Paragi, Gábor and Rákhely, Gábor and Tóth, András},
	doi = {10.1016/j.bbabio.2020.148337},
	journal-iso = {BBA-BIOENERGETICS},
	journal = {BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS},
	volume = {1862},
	unique-id = {31719460},
	issn = {0005-2728},
	year = {2021},
	eissn = {1879-2650},
	orcid-numbers = {Paragi, Gábor/0000-0001-5408-1748; Rákhely, Gábor/0000-0003-2557-3641}
}

@{MTMT:32588990,
	title = {Egy VI. típusú szulfid kinon oxidoreduktáz enzim aktív centrumában található konzervált aminosavak szerepének vizsgálata},
	url = {https://m2.mtmt.hu/api/publication/32588990},
	author = {Turcsik, Dániel},
	booktitle = {Az SZTE Természettudományi és Informatikai Kar Biotechnológiai Tanszékén védett hallgatók munkáinak rezümékötete 2020},
	unique-id = {32588990},
	year = {2020},
	pages = {18}
}

@{MTMT:32588921,
	title = {Kinon kötőhely kialakításában részt vevő aminosavak vizsgálata a Thiocapsa roseopersicina VI. típusú szulfid kinon oxidoreduktáz enzimében},
	url = {https://m2.mtmt.hu/api/publication/32588921},
	author = {Faddi, Izabella},
	booktitle = {Az SZTE Természettudományi és Informatikai Kar Biotechnológiai Tanszékén védett hallgatók munkáinak rezümékötete 2020},
	unique-id = {32588921},
	year = {2020},
	pages = {6}
}

@article{MTMT:31377384,
	title = {Combination of Alanine and Glutathione as Targeting Ligands of Nanoparticles Enhances Cargo Delivery into the Cells of the Neurovascular Unit},
	url = {https://m2.mtmt.hu/api/publication/31377384},
	author = {Porkoláb, Gergő and Mészáros, Mária and Tóth, András and Szecskó, Anikó and Harazin, András and Szegletes, Zsolt and Ferenc, Györgyi and Blastyák, András and Mátés, Lajos and Rákhely, Gábor and Deli, Mária Anna and Veszelka, Szilvia},
	doi = {10.3390/pharmaceutics12070635},
	journal-iso = {PHARMACEUTICS},
	journal = {PHARMACEUTICS},
	volume = {12},
	unique-id = {31377384},
	issn = {1999-4923},
	year = {2020},
	eissn = {1999-4923},
	orcid-numbers = {Harazin, András/0000-0002-0904-5606; Szegletes, Zsolt/0000-0003-2202-6933; Ferenc, Györgyi/0000-0002-3456-319X; Rákhely, Gábor/0000-0003-2557-3641; Deli, Mária Anna/0000-0001-6084-6524}
}

@{MTMT:32588533,
	title = {Egy konzervált glutaminsav szerepének vizsgálata a Thiocapsa roseopersicina VI. típusú szulfid kinon oxidoreduktáz enzimének működésében},
	url = {https://m2.mtmt.hu/api/publication/32588533},
	author = {Dósa, Ildikó},
	booktitle = {Az SZTE Természettudományi és Informatikai Kar Biotechnológiai Tanszékén védett hallgatók munkáinak rezümékötete 2019},
	unique-id = {32588533},
	year = {2019},
	pages = {9}
}

@{MTMT:32588498,
	title = {Szénhidrogének biodegradációja extremofil baktériumokkal},
	url = {https://m2.mtmt.hu/api/publication/32588498},
	author = {Bende, Viktor},
	booktitle = {Az SZTE Természettudományi és Informatikai Kar Biotechnológiai Tanszékén védett hallgatók munkáinak rezümékötete 2019},
	unique-id = {32588498},
	year = {2019},
	pages = {6}
}

@inproceedings{MTMT:30736211,
	title = {Novel sulfide oxidase enzyme candidating for biological treatment of sulfide contaminated water},
	url = {https://m2.mtmt.hu/api/publication/30736211},
	author = {Miklovics, Nikolett and Duzs, Ágnes and Dósa, Ildikó and Rákhely, Gábor and Tóth, András},
	booktitle = {II. Sustainable Raw Materials Conference Book - International Project Week and Scientific Conference},
	unique-id = {30736211},
	year = {2019},
	pages = {212-215},
	orcid-numbers = {Rákhely, Gábor/0000-0003-2557-3641}
}

@{MTMT:32587974,
	title = {Egy VI. típusú szulfid kinon oxidoreduktáz enzim C-terminális doménjének funkcionális vizsgálata},
	url = {https://m2.mtmt.hu/api/publication/32587974},
	author = {Balogh, Fanni},
	booktitle = {Az SZTE Természettudományi és Informatikai Kar Biotechnológiai Tanszékén védett hallgatók munkáinak rezümékötete 2018},
	unique-id = {32587974},
	year = {2018},
	pages = {4}
}