TY - JOUR AU - Bérczi, Alajos AU - Márton, Zsuzsanna AU - Laskay, Krisztina AU - Tóth, András AU - Rákhely, Gábor AU - Duzs, Ágnes AU - Sebőkné Nagy, Krisztina AU - Páli, Tibor AU - Zimányi, László TI - Spectral and Redox Properties of a Recombinant Mouse Cytochrome b561 Protein Suggest Transmembrane Electron Transfer Function JF - MOLECULES J2 - MOLECULES VL - 28 PY - 2023 IS - 5 PG - 16 SN - 1420-3049 DO - 10.3390/molecules28052261 UR - https://m2.mtmt.hu/api/publication/33687467 ID - 33687467 N1 - Funding Agency and Grant Number: Economic Development Operational Program of Hungary [GINOP 2.3.2-15-2016-00001, GINOP 2.3.2-15-2016-00060]; National Research, Development and Innovation Office of Hungary [OTKA K-108697, OTKA K-116323] Funding text: This research was funded by the Economic Development Operational Program of Hungary, grant numbers GINOP 2.3.2-15-2016-00001 and GINOP 2.3.2-15-2016-00060, as well as by the National Research, Development and Innovation Office of Hungary, grant numbers OTKA K-108697 and OTKA K-116323. AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Miklovics, Nikolett AU - Duzs, Ágnes AU - Balogh, Fanni AU - Paragi, Gábor AU - Rákhely, Gábor AU - Tóth, András TI - Quinone binding site in a type VI sulfide:quinone oxidoreductase JF - APPLIED MICROBIOLOGY AND BIOTECHNOLOGY J2 - APPL MICROBIOL BIOT VL - 106 PY - 2022 IS - 22 SP - 7505 EP - 7517 PG - 13 SN - 0175-7598 DO - 10.1007/s00253-022-12202-8 UR - https://m2.mtmt.hu/api/publication/33181371 ID - 33181371 N1 - Funding Agency and Grant Number: ELKH Biological Research Center; European Social Fund [EFOP-3.6.2-16-201700010, GINOP-2.3.2-15-2016-00036]; New National Excellence Program of the Ministry for Innovation and Technology [UNKP-19-3]; State of Hungary Funding text: Open access funding provided by ELKH Biological Research Center. This work headed by GR was supported by the State of Hungary, co-financed by the European Social Fund (EFOP-3.6.2-16-201700010). GP received funding from GINOP-2.3.2-15-2016-00036. NM was supported by the UNKP-19-3 New National Excellence Program of the Ministry for Innovation and Technology. AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Duzs, Ágnes AU - Miklovics, Nikolett AU - Paragi, Gábor AU - Rákhely, Gábor AU - Tóth, András TI - Insights into the catalytic mechanism of type VI sulfide:quinone oxidoreductases JF - BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS J2 - BBA-BIOENERGETICS VL - 1862 PY - 2021 IS - 2 PG - 12 SN - 0005-2728 DO - 10.1016/j.bbabio.2020.148337 UR - https://m2.mtmt.hu/api/publication/31719460 ID - 31719460 N1 - Export Date: 14 September 2022 CODEN: BBBEB LA - English DB - MTMT ER - TY - CHAP AU - Turcsik, Dániel ED - Tóth, András / Selected by ED - Perei, Katalin TI - Egy VI. típusú szulfid kinon oxidoreduktáz enzim aktív centrumában található konzervált aminosavak szerepének vizsgálata T2 - Az SZTE Természettudományi és Informatikai Kar Biotechnológiai Tanszékén védett hallgatók munkáinak rezümékötete 2020 PB - SZTE Természettudományi és Informatikai Kar Biotechnológiai Tanszék CY - Szeged PY - 2020 SP - 18 UR - https://m2.mtmt.hu/api/publication/32588990 ID - 32588990 LA - Hungarian DB - MTMT ER - TY - CHAP AU - Faddi, Izabella ED - Tóth, András / Selected by ED - Perei, Katalin TI - Kinon kötőhely kialakításában részt vevő aminosavak vizsgálata a Thiocapsa roseopersicina VI. típusú szulfid kinon oxidoreduktáz enzimében T2 - Az SZTE Természettudományi és Informatikai Kar Biotechnológiai Tanszékén védett hallgatók munkáinak rezümékötete 2020 PB - SZTE Természettudományi és Informatikai Kar Biotechnológiai Tanszék CY - Szeged PY - 2020 SP - 6 UR - https://m2.mtmt.hu/api/publication/32588921 ID - 32588921 LA - Hungarian DB - MTMT ER - TY - JOUR AU - Porkoláb, Gergő AU - Mészáros, Mária AU - Tóth, András AU - Szecskó, Anikó AU - Harazin, András AU - Szegletes, Zsolt AU - Ferenc, Györgyi AU - Blastyák, András AU - Mátés, Lajos AU - Rákhely, Gábor AU - Deli, Mária Anna AU - Veszelka, Szilvia TI - Combination of Alanine and Glutathione as Targeting Ligands of Nanoparticles Enhances Cargo Delivery into the Cells of the Neurovascular Unit JF - PHARMACEUTICS J2 - PHARMACEUTICS VL - 12 PY - 2020 IS - 7 PG - 23 SN - 1999-4923 DO - 10.3390/pharmaceutics12070635 UR - https://m2.mtmt.hu/api/publication/31377384 ID - 31377384 N1 - These authors contributed equally to this manuscript. (Porkoláb G and Mészáros M) LA - English DB - MTMT ER - TY - CHAP AU - Dósa, Ildikó ED - Tóth, András / Selected by ED - Perei, Katalin TI - Egy konzervált glutaminsav szerepének vizsgálata a Thiocapsa roseopersicina VI. típusú szulfid kinon oxidoreduktáz enzimének működésében T2 - Az SZTE Természettudományi és Informatikai Kar Biotechnológiai Tanszékén védett hallgatók munkáinak rezümékötete 2019 PB - SZTE Természettudományi és Informatikai Kar Biotechnológiai Tanszék CY - Szeged PY - 2019 SP - 9 UR - https://m2.mtmt.hu/api/publication/32588533 ID - 32588533 LA - Hungarian DB - MTMT ER - TY - CHAP AU - Bende, Viktor ED - Tóth, András / Selected by ED - Perei, Katalin TI - Szénhidrogének biodegradációja extremofil baktériumokkal T2 - Az SZTE Természettudományi és Informatikai Kar Biotechnológiai Tanszékén védett hallgatók munkáinak rezümékötete 2019 PB - SZTE Természettudományi és Informatikai Kar Biotechnológiai Tanszék CY - Szeged PY - 2019 SP - 6 UR - https://m2.mtmt.hu/api/publication/32588498 ID - 32588498 LA - Hungarian DB - MTMT ER - TY - CHAP AU - Miklovics, Nikolett AU - Duzs, Ágnes AU - Dósa, Ildikó AU - Rákhely, Gábor AU - Tóth, András ED - Rákhely, Gábor ED - Hodúr, Cecilia TI - Novel sulfide oxidase enzyme candidating for biological treatment of sulfide contaminated water T2 - II. Sustainable Raw Materials Conference Book - International Project Week and Scientific Conference PB - University of Szeged CY - Szeged SN - 9789633066720 PY - 2019 SP - 212 EP - 215 PG - 4 UR - https://m2.mtmt.hu/api/publication/30736211 ID - 30736211 LA - English DB - MTMT ER - TY - CHAP AU - Balogh, Fanni ED - Tóth, András / Selected by ED - Perei, Katalin TI - Egy VI. típusú szulfid kinon oxidoreduktáz enzim C-terminális doménjének funkcionális vizsgálata T2 - Az SZTE Természettudományi és Informatikai Kar Biotechnológiai Tanszékén védett hallgatók munkáinak rezümékötete 2018 PB - SZTE Természettudományi és Informatikai Kar Biotechnológiai Tanszék CY - Szeged PY - 2018 SP - 4 UR - https://m2.mtmt.hu/api/publication/32587974 ID - 32587974 LA - Hungarian DB - MTMT ER -