Substrate-dependent modulation of the enzymatic catalytic activity: Reduction of nitrate, chlorate and perchlorate by respiratory nitrate reductase from Marinobacter hydrocarbonoclasticus 617
Open accessAbstract
The respiratory nitrate reductase complex (NarGHI) from Marinobacter hydrocarbonoclasticus 617 (Mh, formerly Pseudomonas nautica 617) catalyzes the reduction of nitrate to nitrite. This reaction is the first step of the denitrification pathway and is coupled to the quinone pool oxidation and proton translocation to the periplasm, which generates the proton motive force needed for ATP synthesis. The Mh NarGH water-soluble heterodimer has been purified and the kinetic and redox properties have been studied through in-solution enzyme kinetics, protein film voltammetry and spectropotentiometric redox titration. The kinetic parameters of Mh NarGH toward substrates and inhibitors are consistent with those reported for other respiratory nitrate reductases. Protein film voltammetry showed that at least two catalytically distinct forms of the enzyme, which depend on the applied potential, are responsible for substrate reduction. These two forms are affected differentially by the oxidizing substrate, as well as by pH and inhibitors. A new model for the potential dependence of the catalytic efficiency of Nars is proposed.
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PFV experiments on Nap and Nar enzymes reveal different kinetic parameters.
“PFV experiments on Nap and Nar enzymes reveal different kinetic parameters.217–220”
From Nitrate and periplasmic nitrate reductases (2014) · cites this paper as [219]
The NarGHI complex from Marinobacter hydrocarbonoclasticus exhibits a substrate dependent catalysis.
“the NarGHI complex from Marinobacter hydrocarbonoclasticus exhibits a substrate dependent catalysis”
From Nitrate and periplasmic nitrate reductases (2014) · cites this paper as [219]
There is a redox switch between the two states, termed "catalytic" and "boost", which are essentially the Mo(iv) state and Mo(v) states, respectively.
“There is a redox switch between the two states, termed as “catalytic” and “boost” which are essentially the Mo(iv) state and Mo(v) states, respectively.”
From Nitrate and periplasmic nitrate reductases (2014) · cites this paper as [219]
The enzyme-substrate complex formation precedes electron transfer in the NarGHI complex from Marinobacter hydrocarbonoclasticus.
“implying that the enzyme–substrate complex formation precedes electron transfer (Fig. 11).219”
From Nitrate and periplasmic nitrate reductases (2014) · cites this paper as [219]
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- Authors
- Marangon, J., Paes de Sousa, P. M., Moura, I., Brondino, C. D., Moura, J. J. G., & González, P. J.
- Affiliations
- Universidade Nova de Lisboa (PT)
- Universidad Nacional del Litoral (AR)
- Corresponding author
- Moura, José J.G.
- González, Pablo J.
- Venue
- Biochimica et Biophysica Acta (BBA) - Bioenergetics
- Publisher
- Elsevier BV
- Published
- 2012-07
- Volume
- 1817
- Issue
- 7
- Pages
- 1072-1082
- ISSN
- 0005-2728 (ISSN-L)
- OpenAlex
- W2054428479
- Cited by
- 40
- References
- 38
- Citations by year
- 2026: 4 · 2024: 2 · 2023: 2 · 2022: 1 · 2021: 5 · 2020: 4 · 2019: 1 · 2018: 5 · 2017: 4 · 2016: 1 · 2015: 5 · 2014: 2 · 2013: 4
- FWCI
- 1.35
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Bioenergetics (publishedVersion)
- PubMed (publishedVersion)
- CONICET Digital (CONICET) (submittedVersion, cc-by-nc-sa)
- Funders
- Consejo Nacional de Investigaciones Científicas y Técnicas
- Fundação para a Ciência e a Tecnologia (PEst-C/EQB/LA0006/2011, Ciência 2007, Ciência 2008, SFRH/BD/60725/2009, PEst-C/EQB/LA0006/, /2009)
- Topics
- Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
- Physical Sciences › Environmental Science › Environmental Engineering › Microbial Fuel Cells and Bioremediation
- Physical Sciences › Environmental Science › Pollution › Wastewater Treatment and Nitrogen Removal
- Keywords
- respiratory nitrate reductase, Marinobacter hydrocarbonoclasticus, nitrate reduction, chlorate reduction, perchlorate reduction, enzyme kinetics, redox titration, protein film voltammetry, denitrification, quinone pool, proton translocation
- MeSH terms
- Adsorption, Azides, Chlorates, Electrodes, Electron Spin Resonance Spectroscopy, Escherichia coli, Graphite, Hydrogen-Ion Concentration, Kinetics, Models, Biological, Nitrates, Oxidation-Reduction, Perchlorates, Solutions, Spectrophotometry, Substrate Specificity, Crystallography, X-Ray, Nitrate Reductase, Marinobacter, Biocatalysis, Protein Multimerization, Electrochemical Techniques
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