Properties of a Thermostable Nitrate Reductase from the Hyperthermophilic Archaeon Pyrobaculum aerophilum
Open accessAbstract
The nitrate reductase of the hyperthermophilic archaeon Pyrobaculum aerophilum was purified 137-fold from the cytoplasmic membrane. Based on sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis, the enzyme complex consists of three subunits with apparent molecular weights of 130,000, 52,000, and 32,000. The enzyme contained molybdenum (0.8-mol/mol complex), iron (15.4-mol/mol complex) and cytochrome b (0.49-mol/mol complex) as cofactors. The P. aerophilum nitrate reductase distinguishes itself from nitrate reductases of mesophilic bacteria and archaea by its very high specific activity using reduced benzyl viologen as the electron donor ( V max with nitrate, 1,162 s −1 (326 U/mg); V max with chlorate, 1,348 s −1 (378 U/mg) [assayed at 75°C]). The K m values for nitrate and chlorate were 58 and 140 μM, respectively. Azide was a competitive inhibitor and cyanide was a noncompetitive inhibitor of the nitrate reductase activity. The temperature optimum for activity was >95°C. When incubated at 100°C, the purified nitrate reductase had a half-life of 1.5 h. This study constitutes the first description of a nitrate reductase from a hyperthermophilic archaeon.
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The W-containing nitrate reductase from Pyrobaculum aerophilum, purified from cells grown in the presence of Mo and W, was reported to contain mostly Mo.
“purified from cells grown in the presence of Mo and W, was reported to contain mostly Mo”
From Nitrate and periplasmic nitrate reductases (2014) · cites this paper as [208]
A functional W-containing nitrate reductase (Nar) has been isolated from an Achaea, Pyrobaculum aerophilum.
“a functional W-containing nitrate reductase (Nar) has been isolated from an Achaea, Pyrobaculum aerophilum.208”
From Nitrate and periplasmic nitrate reductases (2014) · cites this paper as [208]
There is a natural selection of Mo in nitrate reductases.
“indicating a natural selection of Mo in nitrate reductases.208,209”
From Nitrate and periplasmic nitrate reductases (2014) · cites this paper as [208]
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Cites
Cell biology and molecular basis of denitrification
Zumft, W. G. (1997) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.61.4.533-616.1997 · Cited by 3,483 · see citing works
Berks, B. C., Ferguson, S. J., Moir, J. W. B., & Richardson, D. J. (1995) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(95)00092-5 · Cited by 596 · see citing works
Tungsten in biological systems
Kletzin, A., & Adams, M. W. W. (1996) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.1996.tb00226.x · Cited by 361 · see citing works
Pyrobaculum aerophilum sp. nov., a novel nitrate-reducing hyperthermophilic archaeum
V�lkl, P., Huber, R., Drobner, E., Rachel, R., Burggraf, S., Trincone, A., & STETTER, K. O. (1993) · Applied and Environmental Microbiology · doi:10.1128/aem.59.9.2918-2926.1993 · Cited by 291 · see citing works
Purification and Characterization of the Selenate Reductase from Thauera selenatis
Schröder, I., Rech, S., Krafft, T., & Macy, J. M. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.38.23765 · Cited by 239 · see citing works
Self-citationBlasco, F., Iobbi‐Nivol, C., Ratouchniak, J., Bonnefoy, V., & Chippaux, M. (1990) · Molecular and General Genetics MGG · doi:10.1007/bf00283030 · Cited by 168 · see citing works
CRASKE, A. L., & Ferguson, S. J. (1986) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1986.tb09771.x · Cited by 131 · see citing works
Kinetic analysis of respiratory nitrate reductase from Escherichia coli K12
Morpeth, F. F., & Boxer, D. H. (1985) · Biochemistry · doi:10.1021/bi00322a007 · Cited by 104 · see citing works
Enoch, H. G., & Lester, R. L. (1972) · Journal of Bacteriology · doi:10.1128/jb.110.3.1032-1040.1972 · Cited by 94 · see citing works
10 The Analysis of Cytochromes
Jones, C. W., & Poole, R. K. (1985) · Methods in microbiology · doi:10.1016/s0580-9517(08)70479-3 · Cited by 77 · see citing works
Vorholt, J. A., Hafenbradl, D., STETTER, K. O., & Thauer, R. K. (1997) · Archives of Microbiology · doi:10.1007/s002030050411 · Cited by 71 · see citing works
Kujo, C., & Ohshima, T. (1998) · Applied and Environmental Microbiology · doi:10.1128/aem.64.6.2152-2157.1998 · Cited by 64 · see citing works
Yoshimatsu, K., Sakurai, T., & Fujiwara, T. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01321-1 · Cited by 62 · see citing works
Effect of Tungstate on Nitrate Reduction by the Hyperthermophilic Archaeon Pyrobaculum aerophilum
Afshar, S., Kim, C., Monbouquette, H. G., & Schröder, I. (1998) · Applied and Environmental Microbiology · doi:10.1128/aem.64.8.3004-3008.1998 · Cited by 50 · see citing works
Self-citationThe Purification and Properties of a Copper Nitrite Reductase from Haloferax denitrificans
Inatomi, K.-I., & Hochstein, L. I. (1996) · Current Microbiology · doi:10.1007/s002849900013 · Cited by 48 · see citing works
Blümle, S., & Zumft, W. G. (1991) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(05)80089-1 · Cited by 46 · see citing works
Purification and further characterization of the second nitrate reductase of Escherichia coli K12
Iobbi‐Nivol, C., Santini, C., Blasco, F., & Giordano, G. (1990) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1990.tb15450.x · Cited by 44 · see citing works
Purification and properties of a dissimilatory nitrate reductase from Haloferax denitrificans
Hochstein, L. I., & Lang, F. (1991) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(91)90210-a · Cited by 41 · see citing works
Properties of a Dissimilatory Nitrate Reductase from the Halophilic Archaeon Haloferax volcanii
Bickel‐Sandkötter, S., & Ufer, M. (1995) · Zeitschrift für Naturforschung C · doi:10.1515/znc-1995-5-606 · Cited by 33 · see citing works
Alvarez-Ossorio, M. C., Muriana, F. J. G., de la Rosa, F. F., & Relimpio, A. M. (1992) · Zeitschrift für Naturforschung C · doi:10.1515/znc-1992-9-1005 · Cited by 26 · see citing works
Muriana, F. J. G., Alvarez-Ossorio, M. C., & Relimpio, A. M. (1991) · Biochemical Journal · doi:10.1042/bj2780149 · Cited by 26 · see citing works
Purification, properties and limited proteolysis of nitrate reductase from Pseudomonas denitrificans
Ishizuka, M., Toraya, T., & Fukui, S. (1984) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(84)90082-7 · Cited by 21 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
The mononuclear molybdenum enzymes
Hille, R., Hall, J., & Basu, P. (2014) · Chemical Reviews · doi:10.1021/cr400443z · Cited by 1,738 · see citing works
Microbial nitrate respiration – Genes, enzymes and environmental distribution
Kraft, B., Strous, M., & Tegetmeyer, H. E. (2011) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2010.12.025 · Cited by 465 · see citing works
Nitrate and periplasmic nitrate reductases
Sparacino-Watkins, C., Stolz, J. F., & Basu, P. (2014) · Chem. Soc. Rev. · doi:10.1039/c3cs60249d · Cited by 426 · see citing works
Respiratory Transformation of Nitrous Oxide (N2O) to Dinitrogen by Bacteria and Archaea
Zumft, W. G., & Kroneck, P. M. H. (2006) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/s0065-2911(06)52003-x · Cited by 344 · see citing works
Nitrate reduction and the nitrogen cycle in archaea
Cabello, P., Roldán, M. D., & Moreno‐Vivián, C. (2004) · Microbiology · doi:10.1099/mic.0.27303-0 · Cited by 321 · see citing works
The bioinorganic chemistry of tungsten
Bevers, L. E., Hagedoorn, P., & Hagen, W. R. (2008) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2008.01.017 · Cited by 169 · see citing works
The prokaryotic Mo/W-bisPGD enzymes family: A catalytic workhorse in bioenergetic
Grimaldi, S., Schoepp‐Cothenet, B., Ceccaldi, P., Guigliarelli, B., & Magalon, A. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.01.011 · Cited by 159 · see citing works
Saxena, R., Dhakan, D. B., Mittal, P., Waiker, P., Chowdhury, A., Ghatak, A., & Sharma, V. K. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2016.02123 · Cited by 144 · see citing works
A Gene Cluster for Chlorate Metabolism in Ideonella dechloratans
Thorell, H. D., Stenklo, K., Karlsson, J. E., & Nilsson, T. (2003) · Applied and Environmental Microbiology · doi:10.1128/aem.69.9.5585-5592.2003 · Cited by 111 · see citing works
Martínez‐Espinosa, R. M., Dridge, E. J., Bonete, M.-J., Butt, J. N., Butler, C. S., Sargent, F., & Richardson, D. J. (2007) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2007.00887.x · Cited by 110 · see citing works
Nitrate reductases: Structure, functions, and effect of stress factors
Morozkina, E. V., & Zvyagilskaya, R. A. (2007) · Biochemistry (Moscow) · doi:10.1134/s0006297907100124 · Cited by 103 · see citing works
Nitrogen metabolism in haloarchaea
Bonete, M.-J., Martínez‐Espinosa, R. M., Pire, C., Zafrilla, B., & Richardson, D. J. (2008) · Saline Systems · doi:10.1186/1746-1448-4-9 · Cited by 101 · see citing works
Extracellular cytochrome nanowires appear to be ubiquitous in prokaryotes
Baquero, D. P., Cvirkaitė‐Krupovič, V., Hu, S. S., Fields, J. L., Liu, X., Rensing, C., Egelman, E. H., Krupovìč, M., & Wang, F. (2023) · Cell · doi:10.1016/j.cell.2023.05.012 · Cited by 90 · see citing works
(Per)chlorate in Biology on Earth and Beyond
Youngblut, M. D., Wang, O., Barnum, T. P., & Coates, J. D. (2016) · Annual Review of Microbiology · doi:10.1146/annurev-micro-102215-095406 · Cited by 91 · see citing works
Archaea in dry soil environments
Timonen, S., & Bomberg, M. (2009) · Phytochemistry Reviews · doi:10.1007/s11101-009-9137-5 · Cited by 80 · see citing works
Microbial Synthesis and Transformation of Inorganic and Organic Chlorine Compounds
Atashgahi, S., Liebensteiner, M. G., Janssen, D. B., Smidt, H., Stams, A. J. M., & Sipkema, D. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.03079 · Cited by 72 · see citing works
Lledó, B., Martínez‐Espinosa, R. M., Marhuenda-Egea, F. C., & Bonete, M.-J. (2004) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2004.05.007 · Cited by 73 · see citing works
Constructing the wonders of the bacterial world: biosynthesis of complex enzymes
Sargent, F. (2007) · Microbiology · doi:10.1099/mic.0.2006/004762-0 · Cited by 68 · see citing works
Structure and Evolution of Chlorate Reduction Composite Transposons
Clark, I. C., Melnyk, R. A., Engelbrektson, A. L., & Coates, J. D. (2013) · mBio · doi:10.1128/mbio.00379-13 · Cited by 67 · see citing works
Tracking nitrate reducers and denitrifiers in the environment
Philippot, L. (2005) · Biochemical Society Transactions · doi:10.1042/bst0330200 · Cited by 67 · see citing works
Heider, J., Szaleniec, M., Sünwoldt, K., & Boll, M. (2016) · Microbial Physiology · doi:10.1159/000441357 · Cited by 63 · see citing works
Carlson, H. K., Kuehl, J. V., Hazra, A. B., Justice, N. B., Stoeva, M. K., Sczesnak, A., Mullan, M. R., Iavarone, A. T., Engelbrektson, A. L., Price, M. N., et al. (2014) · The ISME Journal · doi:10.1038/ismej.2014.216 · Cited by 62 · see citing works
Fernandes, A. T., Damas, J. M., Todorović, S., Huber, R., Baratto, M. C., Pogni, R., Soares, C. M., & Martins, L. O. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07725.x · Cited by 57 · see citing works
Cozen, A. E., Weirauch, M. T., Pollard, K. S., Bernick, D. L., Stuart, J. M., & Lowe, T. M. (2008) · Journal of Bacteriology · doi:10.1128/jb.00965-08 · Cited by 57 · see citing works
Liebensteiner, M. G., Tsesmetzis, N., Stams, A. J. M., & Lomans, B. P. (2014) · Frontiers in Microbiology · doi:10.3389/fmicb.2014.00428 · Cited by 55 · see citing works
Gates, A. J., Hughes, R. O., Sharp, S. R., Millington, P. D., Nilavongse, A., Cole, J. A., Leach, E.-R., Jepson, B., Richardson, D. J., & Butler, C. S. (2003) · FEMS Microbiology Letters · doi:10.1016/s0378-1097(03)00122-8 · Cited by 53 · see citing works
Molybdenum and tungsten enzymes redox properties – A brief overview
Cordas, C. M., & Moura, J. J. G. (2019) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2019.05.005 · Cited by 52 · see citing works
Yoshimatsu, K., Iwasaki, T., & Fujiwara, T. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02524-3 · Cited by 50 · see citing works
de Vries, S., Strampraad, M. J. F., Shen, L., Moënne‐Loccoz, P., & Schröder, I. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300857200 · Cited by 50 · see citing works
Chu, S., Zhang, D., Wang, D., Zhi, Y., & Zhou, P. (2017) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2017.04.009 · Cited by 48 · see citing works
DMSO Reductase Family: Phylogenetics and Applications of Extremophiles
Miralles‐Robledillo, J. M., Torregrosa‐Crespo, J., Martínez‐Espinosa, R. M., & Pire, C. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20133349 · Cited by 47 · see citing works
General Characteristics and Important Model Organisms
Kletzin, A. (2014) · ASM Press eBooks · doi:10.1128/9781555815516.ch2 · Cited by 45 · see citing works
Methane, arsenic, selenium and the origins of the DMSO reductase family
Wells, M., Kanmanii, N. J., Zadjali, A. M. A., Janečka, J. E., Basu, P., Oremland, R. S., & Stolz, J. F. (2020) · Scientific Reports · doi:10.1038/s41598-020-67892-9 · Cited by 44 · see citing works
Debnar-Daumler, C., Seubert, A., Schmitt, G., & Heider, J. (2013) · Journal of Bacteriology · doi:10.1128/jb.00980-13 · Cited by 40 · see citing works
Feinberg, L. F., & Holden, J. F. (2005) · Journal of Bacteriology · doi:10.1128/jb.188.2.525-531.2006 · Cited by 40 · see citing works
Celis, A. I., Geeraerts, Z., Ngmenterebo, D., Machovina, M. M., Kurker, R. C., Rajakumar, K., Ivancich, A., Rodgers, K. R., Lukat-Rodgers, G. S., & DuBois, J. L. (2014) · Biochemistry · doi:10.1021/bi501184c · Cited by 34 · see citing works
Liebensteiner, M. G., Pinkse, M. W. H., Nijsse, B., Verhaert, P. D. E. M., Tsesmetzis, N., Stams, A. J. M., & Lomans, B. P. (2015) · Environmental Microbiology Reports · doi:10.1111/1758-2229.12335 · Cited by 35 · see citing works
Arias‐Negrete, S., Jiménez-Romero, L. A., Solı́s-Martı́nez, M. O., Ramı́rez-Emiliano, J., Ávila, E. E., & Cuéllar‐Mata, P. (2004) · Analytical Biochemistry · doi:10.1016/j.ab.2004.01.026 · Cited by 34 · see citing works
Impact of the Dimethyl Sulfoxide Reductase Superfamily on the Evolution of Biogeochemical Cycles
Wells, M., Kim, M., Akob, D. M., Basu, P., & Stolz, J. F. (2023) · Microbiology Spectrum · doi:10.1128/spectrum.04145-22 · Cited by 33 · see citing works
Phylogenomic Dating—The Relative Antiquity of Archaeal Metabolic and Physiological Traits
Blank, C. E. (2009) · Astrobiology · doi:10.1089/ast.2008.0248 · Cited by 31 · see citing works
de Vries, S., Momcilovic, M., Strampraad, M. J. F., Whitelegge, J. P., Baghai, A., & Schröder, I. (2010) · Biochemistry · doi:10.1021/bi100974v · Cited by 29 · see citing works
Clark, I. C., Youngblut, M. D., Jacobsen, G. E., Wetmore, K. M., Deutschbauer, A. M., Lucas, L. N., & Coates, J. D. (2015) · Environmental Microbiology · doi:10.1111/1462-2920.13068 · Cited by 27 · see citing works
Ghareib, M., Abu‐Tahon, M. A., Saif, M. M., & Abdallah, W. E. (2016) · PubMed Central · Cited by 20 · see citing works
Pinho, D., Besson, S., Silva, P. J., de Castro, B., & Moura, I. (2005) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2005.02.008 · Cited by 17 · see citing works
Nunoura, T., Sako, Y., Wakagi, T., & Uchida, A. (2003) · Microbiology · doi:10.1099/mic.0.26000-0 · Cited by 16 · see citing works
Romanowska, I., Kwapisz, E., Mitka, M., & Bielecki, S. (2010) · Journal of Industrial Microbiology & Biotechnology · doi:10.1007/s10295-010-0717-6 · Cited by 15 · see citing works
Biological Networks: Comparison, Conservation, and Evolution via Relative Description Length
Chor, B., & Tuller, T. (2007) · Journal of Computational Biology · doi:10.1089/cmb.2007.r018 · Cited by 13 · see citing works
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Clark, I. C., Melnyk, R. A., Youngblut, M. D., Carlson, H. K., Iavarone, A. T., & Coates, J. D. (2015) · mBio · doi:10.1128/mbio.00282-15 · Cited by 12 · see citing works
Haja, D. K., Wu, C.-H., Poole, F. L., Sugar, J., Williams, S. G., Jones, A. K., & Adams, M. W. W. (2019) · Extremophiles · doi:10.1007/s00792-019-01112-9 · Cited by 13 · see citing works
Thermostable properties of the periplasmic selenate reductase from Thauera selenatis
Dridge, E. J., & Butler, C. S. (2010) · Biochimie · doi:10.1016/j.biochi.2010.06.003 · Cited by 12 · see citing works
Karlsson, J. E., & Nilsson, T. (2005) · Protein Expression and Purification · doi:10.1016/j.pep.2005.02.002 · Cited by 10 · see citing works
Antipov, A. N., Morozkina, E. V., Sorokin, D. Y., Golubeva, L. I., Zvyagilskaya, R. A., & L'vov, N. P. (2005) · Biochemistry (Moscow) · doi:10.1007/s10541-005-0186-0 · Cited by 10 · see citing works
Dridge, E. J., Richardson, D. J., Lewis, R. J., & Butler, C. S. (2006) · Biochemical Society Transactions · doi:10.1042/bst0340118 · Cited by 10 · see citing works
Effect of molybdenum and tungsten on the reduction of nitrate in nitrate reductase, a DFT study
Habib, U., & Hoffman, M. (2017) · Chemistry Central Journal · doi:10.1186/s13065-017-0263-7 · Cited by 8 · see citing works
Ntoko, F. A., & Senwo, Z. N. (2012) · Journal of Environmental Science and Health Part A · doi:10.1080/10934529.2012.695572 · Cited by 8 · see citing works
Geißler, A. (2006) · Qucosa (Saxon State and University Library Dresden) · Cited by 8 · see citing works
John, E. S., & Reysenbach, A. (2023) · Systematic and Applied Microbiology · doi:10.1016/j.syapm.2024.126507 · Cited by 7 · see citing works
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Chor, B., & Tuller, T. (2006) · Lecture notes in computer science · doi:10.1007/11732990_3 · Cited by 7 · see citing works
Ferroni, F. M., Rivas, M. G., Rizzi, A. C., Lucca, M. E., Perotti, N. I., & Brondino, C. D. (2011) · BioMetals · doi:10.1007/s10534-011-9442-5 · Cited by 6 · see citing works
Wang, F., Ren, J., Wang, X., Zhang, Y.-W., Liang, S., Geng, K.-H., Wang, L., Cong, Y., Wang, Y., Wang, L. L., et al. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.145967 · Cited by 5 · see citing works
Relativistic effect behind the molybdenum vs . tungsten selectivity in enzymes
Das, U., Das, A., & Das, A. K. (2025) · Dalton Transactions · doi:10.1039/d5dt00001g · Cited by 5 · see citing works
Hyperthermophile-Metal Interactions in Hydrothermal Environments
Menon, A. L., & Adams, M. W. W. (2014) · ASM Press eBooks · doi:10.1128/9781555817190.ch3 · Cited by 4 · see citing works
Saranya, P. E., & SEKARAN, G. (2015) · Journal of the Taiwan Institute of Chemical Engineers · doi:10.1016/j.jtice.2015.09.014 · Cited by 2 · see citing works
Mahor, D., Püschmann, J., van den Haak, M., Kooij, P. J., van den Ouden, D. L. J., Strampraad, M. J. F., Srour, B., & Hagedoorn, P. (2020) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-020-01784-1 · Cited by 2 · see citing works
Nitrate Assimilation in Halophilic Archaea
Bonete, M.-J., Marhuenda-Egea, F. C., Pire, C., Ferrer, J., & Martínez‐Espinosa, R. M. (2004) · Springer eBooks · doi:10.1007/978-3-662-07656-9_13 · Cited by 2 · see citing works
The Physiology and Evolution of Selenite Respiration in Bacteria
Wells, M. (2020) · Cited by 1 · see citing works
Pal, A., & Pal, S. (2023) · BENTHAM SCIENCE PUBLISHERS eBooks · doi:10.2174/9789815080353122010015 · Cited by 1 · see citing works
Enzymes and electron transport in microbial chlorate respiration
Bohlin, J. (2008) · Diva portal (Dalarna University Library) · Cited by 1 · see citing works
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Pérez‐Rodríguez, I. (2012) · Rutgers University Community Repository (Rutgers University) · doi:10.7282/t3h13113 · Cited by 1 · see citing works
Biological Networks: Comparison, Conservation, and Evolutionary Trees (Extended Abstract)
Chor, B., & Tuller, T. (2006)
Nitrate reductase (cytochrome)
(2006) · Springer eBooks · doi:10.1007/3-540-37704-2_3
Schomburg, P. D., & Schomburg, D. I. (2008) · Springer eBooks · doi:10.1007/3-540-37662-3_82
- Authors
- Afshar, S., Johnson, E., de Vries, S., & Schröder, I.
- Affiliations
- University of California, Los Angeles (US)
- <!--label omitted: 2-->Kluyver Department of Biotechnology, Delft University of Technology, 2628 BC Delft, The Netherlands2
- <!--label omitted: 1-->Department of Microbiology and Molecular Genetics, University of California, Los Angeles, California 90095-1489,1 and
- ORCID
- Afshar, Sepideh
- Venue
- Journal of Bacteriology
- Publisher
- American Society for Microbiology
- Published
- 2001-10
- Volume
- 183
- Issue
- 19
- Pages
- 5491-5495
- ISSN
- 0021-9193 (ISSN-L)
- 1098-5530
- PMC
- PMC95438
- OpenAlex
- W2027145676
- Cited by
- 72
- References
- 22
- Citations by year
- 2025: 2 · 2023: 4 · 2020: 3 · 2019: 3 · 2018: 1 · 2017: 3 · 2016: 3 · 2015: 4 · 2014: 6 · 2013: 4 · 2012: 2
- FWCI
- 2.59
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Journal of Bacteriology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
- Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- nitrate reductase, Pyrobaculum aerophilum, hyperthermophilic archaea, thermostable enzymes, enzyme purification, enzyme subunits, molybdenum cofactor, cytochrome b, chlorate reduction, enzyme kinetics, azide inhibition, cyanide inhibition, thermal stability
- MeSH terms
- Enzyme Stability, Hydrogen-Ion Concentration, Kinetics, Molecular Weight, Molybdoferredoxin, Nitrate Reductases, Temperature, Thermoproteaceae, Protein Subunits, Nitrate Reductase
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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