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Adenosine-5′-Phosphosulfate- and Sulfite Reductases Activities of Sulfate-Reducing Bacteria from Various Environments

A comparative study of the kinetic characteristics (specific activity, initial and maximum rate, and affinity for substrates) of key enzymes of assimilatory sulfate reduction (APS reductase and dissimilatory sulfite reductase) in cell-free extracts of sulphate-reducing bacteria (SRB) from various bi...

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Autores principales: Kushkevych, Ivan, Abdulina, Daryna, Kováč, Jozef, Dordević, Dani, Vítězová, Monika, Iutynska, Galyna, Rittmann, Simon K.-M. R.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7357011/
https://www.ncbi.nlm.nih.gov/pubmed/32560561
http://dx.doi.org/10.3390/biom10060921
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author Kushkevych, Ivan
Abdulina, Daryna
Kováč, Jozef
Dordević, Dani
Vítězová, Monika
Iutynska, Galyna
Rittmann, Simon K.-M. R.
author_facet Kushkevych, Ivan
Abdulina, Daryna
Kováč, Jozef
Dordević, Dani
Vítězová, Monika
Iutynska, Galyna
Rittmann, Simon K.-M. R.
author_sort Kushkevych, Ivan
collection PubMed
description A comparative study of the kinetic characteristics (specific activity, initial and maximum rate, and affinity for substrates) of key enzymes of assimilatory sulfate reduction (APS reductase and dissimilatory sulfite reductase) in cell-free extracts of sulphate-reducing bacteria (SRB) from various biotopes was performed. The material for the study represented different strains of SRB from various ecotopes. Microbiological (isolation and cultivation), biochemical (free cell extract preparation) and chemical (enzyme activity determination) methods served in defining kinetic characteristics of SRB enzymes. The determined affinity data for substrates (i.e., sulfite) were 10 times higher for SRB strains isolated from environmental (soil) ecotopes than for strains from the human intestine. The maximum rate of APS reductase reached 0.282–0.862 µmol/min×mg(−1) of protein that is only 10 to 28% higher than similar initial values. The maximum rate of sulfite reductase for corrosive relevant collection strains and SRB strains isolated from heating systems were increased by 3 to 10 times. A completely different picture was found for the intestinal SRB V(max) in the strains Desulfovibrio piger Vib-7 (0.67 µmol/min × mg(−1) protein) and Desulfomicrobium orale Rod-9 (0.45 µmol/min × mg(−1) protein). The determinant in the cluster distribution of SRB strains is the activity of the terminal enzyme of dissimilatory sulfate reduction—sulfite reductase, but not APS reductase. The data obtained from the activity of sulfate reduction enzymes indicated the adaptive plasticity of SRB strains that is manifested in the change in enzymatic activity.
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spelling pubmed-73570112020-07-23 Adenosine-5′-Phosphosulfate- and Sulfite Reductases Activities of Sulfate-Reducing Bacteria from Various Environments Kushkevych, Ivan Abdulina, Daryna Kováč, Jozef Dordević, Dani Vítězová, Monika Iutynska, Galyna Rittmann, Simon K.-M. R. Biomolecules Article A comparative study of the kinetic characteristics (specific activity, initial and maximum rate, and affinity for substrates) of key enzymes of assimilatory sulfate reduction (APS reductase and dissimilatory sulfite reductase) in cell-free extracts of sulphate-reducing bacteria (SRB) from various biotopes was performed. The material for the study represented different strains of SRB from various ecotopes. Microbiological (isolation and cultivation), biochemical (free cell extract preparation) and chemical (enzyme activity determination) methods served in defining kinetic characteristics of SRB enzymes. The determined affinity data for substrates (i.e., sulfite) were 10 times higher for SRB strains isolated from environmental (soil) ecotopes than for strains from the human intestine. The maximum rate of APS reductase reached 0.282–0.862 µmol/min×mg(−1) of protein that is only 10 to 28% higher than similar initial values. The maximum rate of sulfite reductase for corrosive relevant collection strains and SRB strains isolated from heating systems were increased by 3 to 10 times. A completely different picture was found for the intestinal SRB V(max) in the strains Desulfovibrio piger Vib-7 (0.67 µmol/min × mg(−1) protein) and Desulfomicrobium orale Rod-9 (0.45 µmol/min × mg(−1) protein). The determinant in the cluster distribution of SRB strains is the activity of the terminal enzyme of dissimilatory sulfate reduction—sulfite reductase, but not APS reductase. The data obtained from the activity of sulfate reduction enzymes indicated the adaptive plasticity of SRB strains that is manifested in the change in enzymatic activity. MDPI 2020-06-17 /pmc/articles/PMC7357011/ /pubmed/32560561 http://dx.doi.org/10.3390/biom10060921 Text en © 2020 by the authors. 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 (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Kushkevych, Ivan
Abdulina, Daryna
Kováč, Jozef
Dordević, Dani
Vítězová, Monika
Iutynska, Galyna
Rittmann, Simon K.-M. R.
Adenosine-5′-Phosphosulfate- and Sulfite Reductases Activities of Sulfate-Reducing Bacteria from Various Environments
title Adenosine-5′-Phosphosulfate- and Sulfite Reductases Activities of Sulfate-Reducing Bacteria from Various Environments
title_full Adenosine-5′-Phosphosulfate- and Sulfite Reductases Activities of Sulfate-Reducing Bacteria from Various Environments
title_fullStr Adenosine-5′-Phosphosulfate- and Sulfite Reductases Activities of Sulfate-Reducing Bacteria from Various Environments
title_full_unstemmed Adenosine-5′-Phosphosulfate- and Sulfite Reductases Activities of Sulfate-Reducing Bacteria from Various Environments
title_short Adenosine-5′-Phosphosulfate- and Sulfite Reductases Activities of Sulfate-Reducing Bacteria from Various Environments
title_sort adenosine-5′-phosphosulfate- and sulfite reductases activities of sulfate-reducing bacteria from various environments
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7357011/
https://www.ncbi.nlm.nih.gov/pubmed/32560561
http://dx.doi.org/10.3390/biom10060921
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