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How Biology Handles Nitrite
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ADVERTISEMENT RETURN TO ISSUEPREVReviewNEXTHow Biology Handles NitriteLuisa B. Maia and José J. G. Moura*View Author Information REQUIMTE/CQFB, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2829-516 Caparica, Portugal*E-mail: [email protected]Cite this: Chem. Rev. 2014, 114, 10, 5273–5357Publication Date (Web):April 2, 2014Publication History Received20 September 2013Published online2 April 2014Published inissue 28 May 2014https://doi.org/10.1021/cr400518yCopyright © 2014 American Chemical SocietyRIGHTS & PERMISSIONSACS AuthorChoiceArticle Views12561Altmetric-Citations209LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InReddit PDF (19 MB) Get e-AlertsSUBJECTS:Anions,Bioinorganic chemistry,Monomers,Peptides and proteins,Redox reactions Get e-Alerts
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“Broadly, nitrate reduction is classified into three major pathways (Figure 3)[77,195–197]: 1) Respiratory denitrification, catalyzed by membrane-bound nitrate reductase, nar, or periplasmic nap, is the major electrochemical respiratory pathway for bacterial energy generation under hypoxia via generation of a proton motive force, serving as a two-electron sink in the final step of ATP generation”
From Enterosalivary nitrate metabolism and the microbiome: Intersection of microbial metabolism, nitric oxide and diet in cardiac and pulmonary vascular health (2017) · cites this paper as [197]
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1 retracted
Chandok, M. R., Ytterberg, A. J., van Wijk, K. J., & Klessig, D. F. (2003) · Cell · doi:10.1016/s0092-8674(03)00350-7 · Cited by 176
RetractedNitric oxide: physiology, pathophysiology, and pharmacology.
Moncada, S., Palmer, R. M., & Higgs, E. A. (1991) · Pharmacological Reviews · doi:10.1016/s0031-6997(25)06663-3 · Cited by 15,525
Analysis of nitrate, nitrite, and [15N]nitrate in biological fluids
Green, L. C., Wagner, D. A., Glogowski, J. A., Skipper, P. L., Wishnok, J. S., & Tannenbaum, S. R. (1982) · Analytical Biochemistry · doi:10.1016/0003-2697(82)90118-x · Cited by 12,061
Hydroperoxide metabolism in mammalian organs.
Chance, B., Sies, H., & Boveris, A. (1979) · Physiological Reviews · doi:10.1152/physrev.1979.59.3.527 · Cited by 5,827
Nitric oxide, superoxide, and peroxynitrite: the good, the bad, and ugly
Beckman, J. S., & Koppenol, W. H. (1996) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1996.271.5.c1424 · Cited by 5,513
Oxygen-Derived Free Radicals in Postischemic Tissue Injury
Epstein, F. H., & McCord, J. M. (1985) · New England Journal of Medicine · doi:10.1056/nejm198501173120305 · Cited by 5,399
Nitrogen cycles: Past, present, and future
Galloway, J. N., Dentener, F. J., Capone, D. G., Boyer, E. W., Howarth, R. W., Seitzinger, S. P., Asner, G. P., Cleveland, C. C., Green, P. A., Holland, E. A., et al. (2004) · Biogeochemistry · doi:10.1007/s10533-004-0370-0 · Cited by 5,315
Induction of Apoptotic Program in Cell-Free Extracts: Requirement for dATP and Cytochrome c
Liu, X., Kim, C. N., Yang, J., Jemmerson, R., & Wang, X. (1996) · Cell · doi:10.1016/s0092-8674(00)80085-9 · Cited by 5,167
Prevention of Apoptosis by Bcl-2: Release of Cytochrome c from Mitochondria Blocked
Yang, J., Liu, X., Bhalla, K. N., Kim, C. N., Ibrado, A. M., Cai, J., Peng, T.-I., Jones, D. P., & Wang, X. (1997) · Science · doi:10.1126/science.275.5303.1129 · Cited by 4,913
The Release of Cytochrome c from Mitochondria: A Primary Site for Bcl-2 Regulation of Apoptosis
Kluck, R. M., Bossy‐Wetzel, E., Green, D. R., & Newmeyer, D. D. (1997) · Science · doi:10.1126/science.275.5303.1132 · Cited by 4,715
Nitric oxide synthases: structure, function and inhibition
ALDERTON, W. K., COOPER, C. E., & KNOWLES, R. G. (2001) · Biochemical Journal · doi:10.1042/bj3570593 · Cited by 4,110
The Free Radical Theory of Aging Matures
BECKMAN, K. B., & AMES, B. N. (1998) · Physiological Reviews · doi:10.1152/physrev.1998.78.2.547 · Cited by 3,879
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 3,560
Isolation of an autotrophic ammonia-oxidizing marine archaeon
Könneke, M., Bernhard, A. E., de la Torre, J. R., Walker, C. B., Waterbury, J. B., & Stahl, D. A. (2005) · Nature · doi:10.1038/nature03911 · Cited by 2,864
The nitrate-nitrite-nitric oxide pathway in physiology and therapeutics
Lundberg, J. O., Weitzberg, E., & Gladwin, M. T. (2008) · Nature Reviews Drug Discovery · doi:10.1038/nrd2466 · Cited by 2,739
The Evolution and Future of Earth’s Nitrogen Cycle
Canfield, D. E., Glazer, A. N., & Falkowski, P. G. (2010) · Science · doi:10.1126/science.1186120 · Cited by 2,697
Handbook of methods for oxygen radical research
Greenwald, R. A. (1987) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(87)80012-6 · Cited by 2,388
The Whole Structure of the 13-Subunit Oxidized Cytochrome c Oxidase at 2.8 Å
Tomitake Tsukihara, A., Aoyama, H., Yamashita, E., Tomizaki, T., Yamaguchi, H., Shinzawa‐Itoh, K., Nakashima, R., Yaono, R., & Yoshikawa, S. (1996) · Science · doi:10.1126/science.272.5265.1136 · Cited by 2,102
Mitochondria, oxidative stress and cell death
Ott, M., Gogvadze, V. G., Orrenius, S., & Zhivotovsky, B. (2007) · APOPTOSIS · doi:10.1007/s10495-007-0756-2 · Cited by 2,020
Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
Iwata, S., Ostermeier, C., Ludwig, B., & Michel, H. (1995) · Nature · doi:10.1038/376660a0 · Cited by 2,019
Nitrite-driven anaerobic methane oxidation by oxygenic bacteria
Ettwig, K. F., Butler, M. K., Paslier, D. L., Pelletier, É., Mangenot, S., Kuypers, M. M. M., Schreiber, F., Dutilh, B. E., Zedelius, J., de Beer, D., et al. (2010) · Nature · doi:10.1038/nature08883 · Cited by 1,864
Nitric oxide functions as a signal in plant disease resistance
Delledonne, M., Xia, Y., Dixon, R. A., & Lamb, C. J. (1998) · Nature · doi:10.1038/29087 · Cited by 1,859
Nitrite reduction to nitric oxide by deoxyhemoglobin vasodilates the human circulation
Cosby, K., Partovi, K. S., Crawford, J. H., Patel, R. P., Reiter, C. D., Martyr, S., Yang, B. K., Waclawiw, M. A., Zalos, G., Xu, X., et al. (2003) · Nature Medicine · doi:10.1038/nm954 · Cited by 1,807
The mononuclear molybdenum enzymes
Hille, R., Hall, J., & Basu, P. (2014) · Chemical Reviews · doi:10.1021/cr400443z · Cited by 1,738
Principles of structure, bonding, and reactivity for metal nitrosyl complexes
Enemark, J. H., & Feltham, R. D. (1974) · Coordination Chemistry Reviews · doi:10.1016/s0010-8545(00)80259-3 · Cited by 1,661
The therapeutic potential of carbon monoxide
Motterlini, R., & Otterbein, L. E. (2010) · Nature Reviews Drug Discovery · doi:10.1038/nrd3228 · Cited by 1,643
Characterization of Ligand Binding by Saturation Transfer Difference NMR Spectroscopy
Mayer, M., & Meyer, B. (1999) · Angewandte Chemie International Edition · doi:10.1002/(sici)1521-3773(19990614)38:12 · Cited by 1,622
Hydrogen peroxide sensing and signaling
Veal, E. A., Day, A. M., & Morgan, B. A. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.03.016 · Cited by 1,604
S-nitrosohaemoglobin: a dynamic activity of blood involved in vascular control
Jia, L., Bonaventura, C., Bonaventura, J., & Stamler, J. S. (1996) · Nature · doi:10.1038/380221a0 · Cited by 1,592
Missing lithotroph identified as new planctomycete
Strous, M., Fuerst, J. A., Kramer, E. H. M., Logemann, S., Gerard Muyzer, C., van de Pas-Schoonen, K. T., Webb, R. I., Kuenen, J. G., & Jetten, M. S. M. (1999) · Nature · doi:10.1038/22749 · Cited by 1,578
The Mononuclear Molybdenum Enzymes
Hille, R. (1996) · Chemical Reviews · doi:10.1021/cr950061t · Cited by 1,501
Formation of nitric oxide-derived inflammatory oxidants by myeloperoxidase in neutrophils
Eiserich, J. P., Hristova, M., Cross, C. E., Jones, A. D., Freeman, B. A., Halliwell, B., & van der Vliet, A. (1998) · Nature · doi:10.1038/34923 · Cited by 1,496
Stamler, J. S., Simon, D. I., Osborne, J. A., Mullins, M. E., Jaraki, O., Michel, T. M., Singel, D. J., & Loscalzo, J. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.1.444 · Cited by 1,471
Mechanisms of cytochrome c release from mitochondria
Garrido, C., Galluzzi, L., Brunet, M., Puig, P., Mirjolet, C., & Kroemer, G. (2006) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401950 · Cited by 1,453
Structures of Metal Sites of Oxidized Bovine Heart Cytochrome c Oxidase at 2.8 Å
Tomitake Tsukihara, A., Aoyama, H., Yamashita, E., Tomizaki, T., Yamaguchi, H., Shinzawa‐Itoh, K., Nakashima, R., Yaono, R., & Yoshikawa, S. (1995) · Science · doi:10.1126/science.7652554 · Cited by 1,415
Detection and Imaging of Nitric Oxide with Novel Fluorescent Indicators: Diaminofluoresceins
Kojima, H., Nakatsubo, N., Kikuchi, K., Kawahara, S., Kirino, Y., Nagoshi, H., Hirata, Y., & Nagano, T. (1998) · Analytical Chemistry · doi:10.1021/ac9801723 · Cited by 1,391
A microbial consortium couples anaerobic methane oxidation to denitrification
Raghoebarsing, A. A., Pol, A., van de Pas-Schoonen, K. T., Smolders, A. J. P., Ettwig, K. F., Rijpstra, W. I. C., Stefan Schouten, A., Damsté, J. S. S., den Camp, H. J. M. O., Jetten, M. S. M., et al. (2006) · Nature · doi:10.1038/nature04617 · Cited by 1,364
Deciphering the evolution and metabolism of an anammox bacterium from a community genome
Strous, M., Pelletier, É., Mangenot, S., Rattei, T., Lehner, A., Taylor, M. W., Horn, M., Daims, H., Mavel, D., Wincker, P., et al. (2006) · Nature · doi:10.1038/nature04647 · Cited by 1,357
Febuxostat Compared with Allopurinol in Patients with Hyperuricemia and Gout
Becker, M. A., Schumacher, H. R., Wortmann, R. L., MacDonald, P. A., Eustace, D., Palo, W. A., Streit, J., & Joseph-Ridge, N. (2005) · New England Journal of Medicine · doi:10.1056/nejmoa050373 · Cited by 1,357
Enzyme promiscuity: A mechanistic and evolutionary perspective
Tawfik, O. K. A. D. S. (2010) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-030409-143718 · Cited by 1,355
The biological chemistry of the elements: the inorganic chemistry of life
(1992) · Choice Reviews Online · doi:10.5860/choice.30-0286 · Cited by 1,326
Defense gene induction in tobacco by nitric oxide, cyclic GMP, and cyclic ADP-ribose
Durner, J., Wendehenne, D., & Klessig, D. F. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.17.10328 · Cited by 1,320
Nitric oxide : biology and pathobiology
Ignarro, L. J. (2000) · Cited by 1,306
Cytochrome c acts as a cardiolipin oxygenase required for release of proapoptotic factors
Kagan, V. E., Tyurin, V. A., Jiang, J., Tyurina, Y. Y., Ritov, V. B., Amoscato, A. A., Osipov, A. N., Belikova, N. A., Kapralov, A. A., Kini, V., et al. (2005) · Nature Chemical Biology · doi:10.1038/nchembio727 · Cited by 1,256
Cleeter, M. W. J., Cooper, J. M., Darley-Usmar, V. M., Moncada, S., & Schapira, A. H. V. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00424-2 · Cited by 1,241
Nitric oxide circulates in mammalian plasma primarily as an S-nitroso adduct of serum albumin.
Stamler, J. S., Jaraki, O., Osborne, J., Simon, D. I., Keaney, J., Vita, J., Singel, D., Valeri, C. R., & Loscalzo, J. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.16.7674 · Cited by 1,238
Hydrogen peroxide and nitric oxide as signalling molecules in plants
Neill, S. J., Desikan, R., Clarke, A., Hurst, R. D., & Hancock, J. T. (2002) · Journal of Experimental Botany · doi:10.1093/jexbot/53.372.1237 · Cited by 1,218
Hydrogen Peroxide: A Signaling Messenger
Stone, J. R., & Yang, S. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.243 · Cited by 1,194
OXYGEN DEFICIENCY AND ROOT METABOLISM: Injury and Acclimation Under Hypoxia and Anoxia
DREW, M. C. (1997) · Annual Review of Plant Physiology and Plant Molecular Biology · doi:10.1146/annurev.arplant.48.1.223 · Cited by 1,186
Superoxide radicals in feline intestinal ischemia
Granger, D. N., Rutili, G., & McCord, J. M. (1981) · Gastroenterology · doi:10.1016/0016-5085(81)90648-x · Cited by 1,184
Anammox bacteria: from discovery to application
Kuenen, J. G. (2008) · Nature Reviews Microbiology · doi:10.1038/nrmicro1857 · Cited by 1,179
Cytochrome c: functions beyond respiration
Ow, Y.-L. P., Green, D. R., Hao, Z., & Mak, T. W. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2434 · Cited by 1,144
Nitrite and nitrate determinations in plasma: a critical evaluation
Moshage, H. J., Kok, B., Huizenga, J. R., & Jansen, P. L. M. (1995) · Clinical Chemistry · doi:10.1093/clinchem/41.6.892 · Cited by 1,094
Red cell membrane: past, present, and future
Mohandas, N., & Gallagher, P. G. (2008) · Blood · doi:10.1182/blood-2008-07-161166 · Cited by 1,089
Delledonne, M., Zeier, J., Marocco, A., & Lamb, C. J. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.231178298 · Cited by 1,083
Webb, A. J., Patel, N., Loukogeorgakis, S., Okorie, M., Aboud, Z., Misra, S., Rashid, R., Miall, P., Deanfield, J., Benjamin, N., et al. (2008) · Hypertension · doi:10.1161/hypertensionaha.107.103523 · Cited by 1,078
Brown, G. C., & Cooper, C. E. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)01290-3 · Cited by 1,055
Blood Flow Regulation by S -Nitrosohemoglobin in the Physiological Oxygen Gradient
Stamler, J. S., Jia, L., Eu, J. P., McMahon, T. J., Demchenko, I. T., Bonaventura, J., Gernert, K., & Piantadosi, C. A. (1997) · Science · doi:10.1126/science.276.5321.2034 · Cited by 1,050
Quantitative Aspects of the Production of Superoxide Anion Radical by Milk Xanthine Oxidase
Fridovich, I. (1970) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62884-4 · Cited by 1,035
Nitrate: Nutrient and Signal for Plant Growth
Crawford, N. M. (1995) · The Plant Cell · doi:10.1105/tpc.7.7.859 · Cited by 1,026
A vertebrate globin expressed in the brain
Burmester, T., Weich, B., Reinhardt, S., & Hankeln, T. (2000) · Nature · doi:10.1038/35035093 · Cited by 1,025
ABA‐induced NO generation and stomatal closure in Arabidopsis are dependent on H 2 O 2 synthesis
Bright, J., Desikan, R., Hancock, J. T., Weir, I. S., & Neill, S. J. (2005) · The Plant Journal · doi:10.1111/j.1365-313x.2005.02615.x · Cited by 1,007
The Biological Chemistry of the Elements: The Inorganic Chemistry of Life
Fraústo da Silva, J. J. R., & Williams, R. J. P. (2001) · doi:10.1093/oso/9780198508472.001.0001 · Cited by 1,005
Mammalian nitric oxide synthases
Stuehr, D. J. (1999) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(99)00016-x · Cited by 996
Cytochrome c release from mitochondria proceeds by a two-step process
Ott, M., Robertson, J. D., Gogvadze, V. G., Zhivotovsky, B., & Orrenius, S. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.241655498 · Cited by 955
Molecular mechanism of anaerobic ammonium oxidation
Kartal, B., Maalcke, W. J., de Almeida, N. M., Cirpus, I. E. Y., Gloerich, J., Geerts, W. J., den Camp, H. J. M. O., Harhangi, H. R., Janssen‐Megens, E. M., Françoijs, K., et al. (2011) · Nature · doi:10.1038/nature10453 · Cited by 952
Berry, C. E., & Hare, J. M. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2003.055913 · Cited by 925
Workgroup Report: Drinking-Water Nitrate and Health—Recent Findings and Research Needs
Ward, M. H., de Kok, T. M. C. M., Levallois, P., Brender, J. D., Guliš, G., Nolan, B. T., & VanDerslice, J. A. (2005) · Environmental Health Perspectives · doi:10.1289/ehp.8043 · Cited by 924
The anaerobic oxidation of ammonium
Jetten, M. S. M., Strous, M., van de Pas-Schoonen, K. T., Schalk, J., van Dongen, U. G. J. M., van de Graaf, A. A., Logemann, S., Muyzer, G., van Loosdrecht, M. C. M., & Kuenen, J. G. (1998) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.1998.tb00379.x · Cited by 909
Superoxide production by the mitochondrial respiratory chain
Turrens, J. F. (1997) · Bioscience Reports · doi:10.1023/a:1027374931887 · Cited by 903
Electronic structures of active sites in copper proteins: contributions to reactivity
Solomon, E. I., Baldwin, M. J., & Lowery, M. D. (1992) · Chemical Reviews · doi:10.1021/cr00012a003 · Cited by 901
The Production of Malignant Primary Hepatic Tumours in the Rat by Feeding Dimethylnitrosamine
Magee, P. N., & Barnes, J. M. (1956) · British Journal of Cancer · doi:10.1038/bjc.1956.15 · Cited by 900
Derelle, É., Ferraz, C., Rombauts, S., Rouzé, P., Worden, A. Z., Robbens, S., Partensky, F., Degroeve, S., Echeynié, S., Cooke, R., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604795103 · Cited by 893
Identification of a Plant Nitric Oxide Synthase Gene Involved in Hormonal Signaling
Guo, F.-Q., Okamoto, M., & Crawford, N. M. (2003) · Science · doi:10.1126/science.1086770 · Cited by 889
The oxidative pentose phosphate pathway: structure and organisation
Kruger, N. J., & von Schaewen, A. (2003) · Current Opinion in Plant Biology · doi:10.1016/s1369-5266(03)00039-6 · Cited by 879
Nitric Oxide: The Versatility of an Extensive Signal Molecule
Lamattina, L., García‐Mata, C., Graziano, M., & Pagnussat, G. C. (2003) · Annual Review of Plant Biology · doi:10.1146/annurev.arplant.54.031902.134752 · Cited by 877
Molybdenum cofactors, enzymes and pathways
Schwarz, G., Mendel, R. R., & Ribbe, M. W. (2009) · Nature · doi:10.1038/nature08302 · Cited by 872
Nitric oxide signalling in plants
Neill, S. J., Desikan, R., & Hancock, J. T. (2003) · New Phytologist · doi:10.1046/j.1469-8137.2003.00804.x · Cited by 872
Clementi, E., Brown, G. C., Feelisch, M., & Moncada, S. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.13.7631 · Cited by 863
Treusch, A. H., Leininger, S., Kletzin, A., Schuster, S. C., Klenk, H., & Schleper, C. (2005) · Environmental Microbiology · doi:10.1111/j.1462-2920.2005.00906.x · Cited by 860
Ignarro, L. J., Fukuto, J. M., Griscavage, J. M., Rogers, N. E., & Byrns, R. E. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.17.8103 · Cited by 856
Methods in nitric oxide research
Feelisch, M., & Stamler, J. S. (1996) · ePrints Soton (University of Southampton) · Cited by 828
Tetrapyrrole Biosynthesis in Higher Plants
Tanaka, R., & Tanaka, A. (2007) · Annual Review of Plant Biology · doi:10.1146/annurev.arplant.57.032905.105448 · Cited by 823
The role of abscisic acid in plant–pathogen interactions
Mauch‐Mani, B., & Mauch, F. (2005) · Current Opinion in Plant Biology · doi:10.1016/j.pbi.2005.05.015 · Cited by 821
Structure and function of xanthine oxidoreductase: where are we now?
Harrison, R. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00956-5 · Cited by 807
Production of NO 2 - and N 2 O by Nitrifying Bacteria at Reduced Concentrations of Oxygen
Goreau, T. J. F., Kaplan, W. A., Wofsy, S. C., McElroy, M. B., Valois, F. W., & Watson, S. W. (1980) · Applied and Environmental Microbiology · doi:10.1128/aem.40.3.526-532.1980 · Cited by 805
Regulation of nitric oxide (NO) production by plant nitrate reductase in vivo and in vitro
Rockel, P., Strube, F., Rockel, A., Wildt, J., & Kaiser, W. M. (2002) · Journal of Experimental Botany · doi:10.1093/jexbot/53.366.103 · Cited by 801
Complex regulation of ABA biosynthesis in plants
Seo, M., & Koshiba, T. (2002) · Trends in Plant Science · doi:10.1016/s1360-1385(01)02187-2 · Cited by 796
Campbell, W. H. (1999) · Annual Review of Plant Physiology and Plant Molecular Biology · doi:10.1146/annurev.arplant.50.1.277 · Cited by 796
Does nitric oxide modulate mitochondrial energy generation and apoptosis?
Moncada, S., & Erusalimsky, J. D. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm762 · Cited by 794
Enzyme-independent formation of nitric oxide in biological tissues
Zweier, J. L., Wang, P., Samouilov, A., & Kuppusamy, P. (1995) · Nature Medicine · doi:10.1038/nm0895-804 · Cited by 788
Mitochondrial control of apoptosis: the role of cytochrome c
Cai, J., Yang, J., & Jones, D. (1998) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(98)00109-1 · Cited by 787
Lücker, S., Wagner, M., Maixner, F., Pelletier, É., Koch, H., Vacherie, B., Rattei, T., Damsté, J. S. S., Spieck, E., Paslier, D. L., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1003860107 · Cited by 784
Formation of reactive nitrogen species during peroxidase-catalyzed oxidation of nitrite
van der Vliet, A., Eiserich, J. P., Halliwell, B., & Cross, C. E. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.12.7617 · Cited by 780
Francis, C. A., Beman, J. M., & Kuypers, M. M. M. (2007) · The ISME Journal · doi:10.1038/ismej.2007.8 · Cited by 775
García‐Mata, C., & Lamattina, L. (2001) · PLANT PHYSIOLOGY · doi:10.1104/pp.126.3.1196 · Cited by 766
Nitric oxide and salicylic acid signaling in plant defense
Klessig, D. F., Durner, J., Noad, R. J., Navarre, D. A., Wendehenne, D., Kumar, D., Zhou, J. M., Shah, J., Zhang, S., Kachroo, P., et al. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.16.8849 · Cited by 765
The biological lifetime of nitric oxide: Implications for the perivascular dynamics of NO and O 2
Thomas, D. D., Liu, X., Kantrow, S. P., & Lancaster, J. R. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.1.355 · Cited by 760
Hyperoxia increases oxygen radical production in rat lungs and lung mitochondria.
Freeman, B. Α., & Crapo, J. D. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)68544-3 · Cited by 752
Nitric oxide, stomatal closure, and abiotic stress
Neill, S. J., Barros, R., Bright, J., Desikan, R., Hancock, J. T., Harrison, J., Morris, P. C., Ribeiro, D. M., & Wilson, I. D. (2008) · Journal of Experimental Botany · doi:10.1093/jxb/erm293 · Cited by 746
Nitrate, bacteria and human health
Lundberg, J. O., Weitzberg, E., Cole, J. A., & Benjamin, N. (2004) · Nature Reviews Microbiology · doi:10.1038/nrmicro929 · Cited by 739
Duncan, C., Dougall, H., Johnston, P., Green, S., Brogan, R., Leifert, C., Smith, L., Golden, M., & Benjamin, N. (1995) · Nature Medicine · doi:10.1038/nm0695-546 · Cited by 734
The Regulation of Rat Liver Xanthine Oxidase
Stirpe, F., Corte, E. D., & Lorenzoni, E. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36428-1 · Cited by 733
Enroth, C., Eger, B. T., Okamoto, K., Nishino, T., Nishino, T., & Pai, E. F. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.20.10723 · Cited by 733
Apoptosis: a basic biological phenomenon with wide‐ranging implications in human disease
Fadeel, B., & Orrenius, S. (2005) · Journal of Internal Medicine · doi:10.1111/j.1365-2796.2005.01570.x · Cited by 727
Farrell, A. J., Blake, D. R., Palmer, R. M. J., & Moncada, S. (1992) · Annals of the Rheumatic Diseases · doi:10.1136/ard.51.11.1219 · Cited by 717
Desikan, R., Griffiths, R., Hancock, J. T., & Neill, S. J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.252461999 · Cited by 711
Kaur, H., & Halliwell, B. B. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00722-5 · Cited by 706
Control of coronary vascular tone by nitric oxide.
Kelm, M., & Schrader, J. (1990) · Circulation Research · doi:10.1161/01.res.66.6.1561 · Cited by 697
Dietary Inorganic Nitrate Improves Mitochondrial Efficiency in Humans
Larsen, F. J., Schiffer, T. A., Borniquel, S., Sahlin, K., Ekblom, B., Lundberg, J. O., & Weitzberg, E. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.01.004 · Cited by 689
Simulation of the diffusion and reaction of endogenously produced nitric oxide.
Lancaster, J. R. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.17.8137 · Cited by 689
A moderately thermophilic ammonia-oxidizing crenarchaeote from a hot spring
Hatzenpichler, R., Lebedeva, E. V., Spieck, E., Stoecker, K., Richter, A. A., Daims, H., & Wagner, M. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0708857105 · Cited by 688
Beligni, M. V., & Lamattina, L. (2000) · Planta · doi:10.1007/pl00008128 · Cited by 680
Leghemoglobin and Rhizobium Respiration
Appleby, C. A. (1984) · Annual Review of Plant Physiology and Plant Molecular Biology · doi:10.1146/annurev.pp.35.060184.002303 · Cited by 679
Ischemia-reperfusion injury: role of oxygen-derived free radicals.
Granger, D. N., Höllwarth, M. E., & Parks, D. A. (1986) · PubMed · Cited by 676
Cytoprotective effects of nitrite during in vivo ischemia-reperfusion of the heart and liver
Duranski, M. R., Greer, J. J. M., Dejam, A., Jaganmohan, S., Hogg, N., Langston, W., Patel, R. P., Yet, S.-F., Wang, X., Kevil, C. G., et al. (2005) · Journal of Clinical Investigation · doi:10.1172/jci22493 · Cited by 674
Green, L. C., Ruiz de Luzuriaga, K., Wagner, D. A., Rand, W., Istfan, N., Young, V. R., & Tannenbaum, S. R. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.12.7764 · Cited by 665
Benjamin, N., O'Driscoll, F., Dougall, H., Duncan, C., Smith, L., Golden, M., & McKenzie, H. (1994) · Nature · doi:10.1038/368502a0 · Cited by 665
Intragastric nitric oxide production in humans: measurements in expelled air.
Lundberg, J. O., Weitzberg, E., Lundberg, J. M., & Alving, K. (1994) · Gut · doi:10.1136/gut.35.11.1543 · Cited by 661
Inorganic nitrate is a possible source for systemic generation of nitric oxide
Lundberg, J. O., & Govoni, M. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.04.027 · Cited by 657
The Assimilatory Nitrate-Reducing System and its Regulation
Guerrero, M. G., Vega, J. M., & Losada, M. (1981) · Annual Review of Plant Physiology · doi:10.1146/annurev.pp.32.060181.001125 · Cited by 651
Poth, M. A., & Focht, D. D. (1985) · Applied and Environmental Microbiology · doi:10.1128/aem.49.5.1134-1141.1985 · Cited by 650
Oxidation of nitrogen-oxides by bound dioxygen in hemoproteins
Doyle, M. P., & Hoekstra, J. W. (1981) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(00)80291-3 · Cited by 643
Effects of dietary nitrate on oxygen cost during exercise
Larsen, F. J., Weitzberg, E., Lundberg, J. O., & Ekblom, B. (2007) · Acta Physiologica · doi:10.1111/j.1748-1716.2007.01713.x · Cited by 637
Genomic studies of uncultivated archaea
Schleper, C., Jurgens, G., & Jonuscheit, M. (2005) · Nature Reviews Microbiology · doi:10.1038/nrmicro1159 · Cited by 635
Inorganic Nitrate Supplementation Lowers Blood Pressure in Humans: Role for Nitrite-Derived NO
Kapil, V., Milsom, A. B., Okorie, M., Maleki-Toyserkani, S., Akram, F., Rehman, F., Arghandawi, S., Pearl, V., Benjamin, N., Loukogeorgakis, S., et al. (2010) · Hypertension · doi:10.1161/hypertensionaha.110.153536 · Cited by 621
The Nucleobase‐Cation‐Symport‐1 Family of Membrane Transport Proteins
Weyand, S. N., Ma, P., Saidijam, M., Baldwin, J. M., Beckstein, O., Jackson, S. M., Suzuki, S., Patching, S. G., Shimamura, T., Sansom, M. S. P., et al. (2004) · Handbook of Metalloproteins · doi:10.1002/0470028637.met268 · Cited by 619
Mechanism of NO-induced oxidation of myoglobin and hemoglobin
Eich, R. F., Li, T., Lemon, D. D., Doherty, D. H., Curry, S. R., Aitken, J. F., Mathews, A. J., Johnson, K. A., Smith, R. D., Phillips, et al. (1996) · Biochemistry · doi:10.1021/bi960442g · Cited by 613
Implication of free radical mechanisms in ethanol-induced cellular injury
Nordmann, R., Ribière, C., & Rouach, H. (1992) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(92)90030-k · Cited by 610
Webb, A., Bond, R., McLean, P., Uppal, R., Benjamin, N., & Ahluwalia, A. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402927101 · Cited by 608
Govoni, M., Jansson, E. Å., Weitzberg, E., & Lundberg, J. O. (2008) · Nitric Oxide · doi:10.1016/j.niox.2008.08.003 · Cited by 602
Zweier, J. L., Kuppusamy, P., & Lutty, G. A. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.11.4046 · Cited by 601
Shiva, S., Huang, Z., Grubina, R., Sun, J., Ringwood, L. A., MacArthur, P. H., Xu, X., Murphy, E., Darley-Usmar, V. M., & Gladwin, M. T. (2007) · Circulation Research · doi:10.1161/01.res.0000260171.52224.6b · Cited by 599
Spiegelhalder, B., Eisenbrand, G., & Preussmann, R. (1976) · Food and Cosmetics Toxicology · doi:10.1016/s0015-6264(76)80005-3 · Cited by 596
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
Nitrate regulation of metabolism and growth
Stitt, M. D. (1999) · Current Opinion in Plant Biology · doi:10.1016/s1369-5266(99)80033-8 · Cited by 588
Effects of Dietary Nitrate on Blood Pressure in Healthy Volunteers
Larsen, F. J., Ekblom, B., Sahlin, K., Lundberg, J. O., & Weitzberg, E. (2006) · New England Journal of Medicine · doi:10.1056/nejmc062800 · Cited by 587
Plasma nitrite reflects constitutive nitric oxide synthase activity in mammals
Kleinbongard, P., Dejam, A., Lauer, T., Rassaf, T., Schindler, A., Picker, O., Scheeren, T., Gödecke, A., Schrader, J., Schulz, R., et al. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(03)00406-4 · Cited by 586
Lauer, T., Preik, M., Rassaf, T., Strauer, B. E., Deussen, A., Feelisch, M., & Kelm, M. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.221381098 · Cited by 585
Wang, R., Guegler, K. J., LaBrie, S. T., & Crawford, N. M. (2000) · The Plant Cell · doi:10.1105/tpc.12.8.1491 · Cited by 585
Carbon Dioxide Enrichment Inhibits Nitrate Assimilation in Wheat and Arabidopsis
Bloom, A. J., Burger, M., Rubio-Asensio, J. S., & Cousins, A. B. (2010) · Science · doi:10.1126/science.1186440 · Cited by 580
Export by red blood cells of nitric oxide bioactivity
Pawloski, J. R., Hess, D. T., & Stamler, J. S. (2001) · Nature · doi:10.1038/35054560 · Cited by 579
Biochemistry and molecular biology of anammox bacteria
Jetten, M. S. M., van Niftrik, L., Strous, M., Kartal, B., Keltjens, J. T., & den Camp, H. J. M. O. (2009) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230902722783 · Cited by 575
Distribution and ecophysiology of the nitrifying bacteria emphasizing cultured species
Koops, H., & Pommerening‐Röser, A. (2001) · FEMS Microbiology Ecology · doi:10.1111/j.1574-6941.2001.tb00847.x · Cited by 573
Hochachka, P. W., & Mommsen, T. P. (1983) · Science · doi:10.1126/science.6298937 · Cited by 572
Nitric oxide: comparative synthesis and signaling in animal and plant cells
Wendehenne, D., Pugin, A., Klessig, D. F., & Durner, J. (2001) · Trends in Plant Science · doi:10.1016/s1360-1385(01)01893-3 · Cited by 571
Nitric oxide dioxygenase: An enzymic function for flavohemoglobin
Gardner, P. R., Gardner, A. M., Martin, L. A., & Salzman, A. L. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.18.10378 · Cited by 569
Kartal, B., Kuypers, M. M. M., Lavik, G., Schalk, J., den Camp, H. J. M. O., Jetten, M. S. M., & Strous, M. (2006) · Environmental Microbiology · doi:10.1111/j.1462-2920.2006.01183.x · Cited by 566
Myoglobin-facilitated oxygen diffusion: role of myoglobin in oxygen entry into muscle.
Wittenberg, J. B. (1970) · Physiological Reviews · doi:10.1152/physrev.1970.50.4.559 · Cited by 565
Nitric Oxide Represses the Arabidopsis Floral Transition
He, Y., Tang, R., Hao, Y., Stevens, R. D., Cook, C. W., Ahn, S. M., Jing, L., Yang, Z., Chen, L., Guo, F., et al. (2004) · Science · doi:10.1126/science.1098837 · Cited by 565
Peroxynitrite reactivity with amino acids and proteins
Alvarez, B., & Radi, R. (2003) · Amino Acids · doi:10.1007/s00726-003-0018-8 · Cited by 560
Superoxide Dismutases: Ancient Enzymes and New Insights
Miller, A.-F. (2012) · FEBS Letters · doi:10.1016/j.febslet.2011.10.048 · Cited by 557
Apoplastic Synthesis of Nitric Oxide by Plant Tissues
Bethke, P. C., Badger, M. R., & Jones, R. L. (2004) · The Plant Cell · doi:10.1105/tpc.017822 · Cited by 557
Linking crenarchaeal and bacterial nitrification to anammox in the Black Sea
Lam, P., Jensen, M. M., Lavik, G., McGinnis, D. F., Müller, B., Schubert, C. J., Amann, R., Thamdrup, B., & Kuypers, M. M. M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0611081104 · Cited by 557
Shiva, S., Sack, M. N., Greer, J. J., Duranski, M., Ringwood, L. A., Burwell, L., Wang, X., MacArthur, P. H., Shoja, A., Raghavachari, N., et al. (2007) · The Journal of Experimental Medicine · doi:10.1084/jem.20070198 · Cited by 555
Chain, P., Lamerdin, J. E., Larimer, F. W., Regala, W., Lao, V., Land, M., Hauser, L., Hooper, A. B., Klotz, M. G., Norton, J. M., et al. (2003) · Journal of Bacteriology · doi:10.1128/jb.185.9.2759-2773.2003 · Cited by 552
Wittenberg, J. B., & Wittenberg, B. A. (2003) · Journal of Experimental Biology · doi:10.1242/jeb.00243 · Cited by 550
Yamasaki, H., & Sakihama, Y. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01203-5 · Cited by 549
Essential Roles of S-Nitrosothiols in Vascular Homeostasis and Endotoxic Shock
Liu, L., Yan, Y., Zeng, M., Zhang, J., Hanes, M. A., Ahearn, G. S., McMahon, T., Dickfeld, T. L., Marshall, H. E., Que, L. G., et al. (2004) · Cell · doi:10.1016/s0092-8674(04)00131-x · Cited by 546
Dissimilatory Nitrite and Nitric Oxide Reductases
Averill, B. A. (1996) · Chemical Reviews · doi:10.1021/cr950056p · Cited by 545
Measurement of Nitric Oxide and Peroxynitrite Generation in the Postischemic Heart
Wang, P., & Zweier, J. L. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.46.29223 · Cited by 542
Nitric Oxide Is a Novel Component of Abscisic Acid Signaling in Stomatal Guard Cells
Neill, S. J., Desikan, R., Clarke, A., & Hancock, J. T. (2002) · PLANT PHYSIOLOGY · doi:10.1104/pp.010707 · Cited by 542
Nitric oxide: a new player in plant signalling and defence responses
Wendehenne, D., Durner, J., & Klessig, D. F. (2004) · Current Opinion in Plant Biology · doi:10.1016/j.pbi.2004.04.002 · Cited by 540
Greenhouse warming by CH 4 in the atmosphere of early Earth
Pavlov, A. A., Kasting, J. F., Brown, L. L., Rages, K. A., & Freedman, R. (2000) · Journal of Geophysical Research: Planets · doi:10.1029/1999je001134 · Cited by 537
Oxidative stress, anti‐oxidant therapies and chronic kidney disease
Small, D. M., Coombes, J. S., Bennett, N. J., Johnson, D. W., & Gobe, G. C. (2012) · Nephrology · doi:10.1111/j.1440-1797.2012.01572.x · Cited by 529
Mechanistic aspects of the reactions of nitric oxide with transition-metal complexes
Ford, P. C., & Lorkovic, I. M. (2002) · Chemical Reviews · doi:10.1021/cr0000271 · Cited by 525
Vascular Oxidative Stress and Endothelial Dysfunction in Patients With Chronic Heart Failure
Landmesser, U., Spiekermann, S., Dikalov, S., Tatge, H., Wilke, R., Kohler, C., Harrison, D. G., Hornig, B., & Drexler, H. (2002) · Circulation · doi:10.1161/01.cir.0000041431.57222.af · Cited by 525
The Molecular Mechanism of the Catalase Reaction
Alfonso‐Prieto, M., Biarnés, X., Vidossich, P., & Rovira, C. (2009) · Journal of the American Chemical Society · doi:10.1021/ja9018572 · Cited by 524
Assimilatory Nitrate Reductase: Functional Properties And Regulation
Solomonson, L. P., & Barber, M. J. (1990) · Annual Review of Plant Physiology and Plant Molecular Biology · doi:10.1146/annurev.pp.41.060190.001301 · Cited by 523
Enzymatic function of hemoglobin as a nitrite reductase that produces NO under allosteric control
Huang, Z. (2005) · Journal of Clinical Investigation · doi:10.1172/jci24650 · Cited by 520
Nitrite is a signaling molecule and regulator of gene expression in mammalian tissues
Bryan, N. S., Fernandez, B. O., Bauer, S. M., Garcia-Saura, M. F., Milsom, A. B., Rassaf, T., Maloney, R. E., Bharti, A., Rodriguez, J., & Feelisch, M. (2005) · Nature Chemical Biology · doi:10.1038/nchembio734 · Cited by 518
ABA, hydrogen peroxide and nitric oxide signalling in stomatal guard cells
Desikan, R. (2003) · Journal of Experimental Botany · doi:10.1093/jxb/erh033 · Cited by 515
Zhao, M., Chen, L., Zhang, L., & Zhang, W. (2009) · PLANT PHYSIOLOGY · doi:10.1104/pp.109.140996 · Cited by 515
Diffusion-limited reaction of free nitric oxide with erythrocytes
Liu, X., Miller, M. J. S., Joshi, M. S., Sadowska-Krowicka, H., Clark, D. A., & Lancaster, J. R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.30.18709 · Cited by 512
Nitric oxide and iron proteins
Cooper, C. E. (1999) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(99)00021-3 · Cited by 510
Reactive oxygen species, antioxidant systems and nitric oxide in peroxisomes
del Río, L. A., Corpas, F. J., Sandalio, L. M., Palma, J. M., Gómez, M., & Barroso, J. B. (2002) · Journal of Experimental Botany · doi:10.1093/jexbot/53.372.1255 · Cited by 507
Polyamines Induce Rapid Biosynthesis of Nitric Oxide (NO) in Arabidopsis thaliana Seedlings
Tun, N. N., Santa‐Catarina, C., Begum, T., Silveira, V., Handro, W., Floh, E. I. S., & Scherer, G. F. E. (2006) · Plant and Cell Physiology · doi:10.1093/pcp/pci252 · Cited by 503
NO news is good news for plants
Delledonne, M. (2005) · Current Opinion in Plant Biology · doi:10.1016/j.pbi.2005.05.002 · Cited by 503
Hypoxia, red blood cells, and nitrite regulate NO-dependent hypoxic vasodilation
Crawford, J. H. (2006) · Blood · doi:10.1182/blood-2005-07-2668 · Cited by 497
Determinants of a protein fold
Bashford, D., Chothia, C., & Lesk, A. M. (1987) · Journal of Molecular Biology · doi:10.1016/0022-2836(87)90521-3 · Cited by 496
Cytoglobin: A Novel Globin Type Ubiquitously Expressed inVertebrate Tissues
Burmester, T., Ebner, B., Weich, B., & Hankeln, T. (2002) · Molecular Biology and Evolution · doi:10.1093/oxfordjournals.molbev.a004096 · Cited by 496
Castello, P. R., David, P. S., McClure, T., Crook, Z., & Poyton, R. O. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.02.011 · Cited by 495
A Tutorial on the Diffusibility and Reactivity of Free Nitric Oxide
Lancaster, J. R. (1997) · Nitric Oxide · doi:10.1006/niox.1996.0112 · Cited by 495
Relevance of nitrosamines to human cancer
Bartsch, H., & Montesano, R. (1984) · Carcinogenesis · doi:10.1093/carcin/5.11.1381 · Cited by 495
The Measurement of Pyridine Nucleotides by Enzymatic Cycling
Lowry, O. H., Passonneau, J. V., Schulz, D. W., & Rock, M. K. (1961) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)61729-1 · Cited by 494
Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A
Bertero, M. G., Rothery, R. A., Palak, M., Hou, C., Lim, D., Blasco, F., Weiner, J. H., & Strynadka, N. C. J. (2003) · Nature Structural & Molecular Biology · doi:10.1038/nsb969 · Cited by 494
Nitric oxide synthesis and signalling in plants
Wilson, I. D., Neill, S. J., & Hancock, J. T. (2007) · Plant Cell & Environment · doi:10.1111/j.1365-3040.2007.01761.x · Cited by 493
Millar, T. M., Stevens, C. R., Benjamin, N., Eisenthal, R., Harrison, R., & Blake, D. R. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00430-x · Cited by 491
Copper Proteins and Copper Enzymes
Lontie, R. (2018) · CRC Press eBooks · doi:10.1201/9781351070898 · Cited by 489
Brennan, M.-L., Wu, W., Fu, X., Shen, Z., Song, W., Frost, H., Vadseth, C., Narine, L., Lenkiewicz, E., Borchers, M. T., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m112400200 · Cited by 486
Guyer, R. L., & Koshland, D. E. (1989) · Science · doi:10.1126/science.2688087 · Cited by 482
Crystal Structure of the Xanthine Oxidase-Related Aldehyde Oxido-Reductase from D. gigas
Romão, M. J., Archer, M., Moura, I., Moura, J. J. G., LeGall, J., Engh, R. A., Schneider, M., Hof, P., & Huber, R. (1995) · Science · doi:10.1126/science.270.5239.1170 · Cited by 481
Self-citationWasser, I. M., de Vries, S., Moënne‐Loccoz, P., Schröder, I., & Karlin, K. D. (2002) · Chemical Reviews · doi:10.1021/cr0006627 · Cited by 481
Wink, D. A., Darbyshire, J. F., Nims, R. W., Saavedra, J. E., & Ford, P. C. (1993) · Chemical Research in Toxicology · doi:10.1021/tx00031a003 · Cited by 480
Refined crystal structure of ascorbate oxidase at 1.9 Å resolution
Messerschmidt, A., Ladenstein, R., Huber, R., Bolognesi, M., Avigliano, L., Petruzzelli, R., Rossi, A., & Finazzi‐Agrò, A. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90583-6 · Cited by 475
Evidence for complete denitrification in a benthic foraminifer
Risgaard‐Petersen, N., Langezaal, A. M., Høgslund, S. M., Schmid, M. C., Jetten, M. S. M., den Camp, H. J. M. O., Derksen, J. W. M., Piña-Ochoa, E., Eriksson, S. P., Nielsen, L. P., et al. (2006) · Nature · doi:10.1038/nature05070 · Cited by 469
Wittenberg, B. A., & Wittenberg, J. B. (1989) · Annual Review of Physiology · doi:10.1146/annurev.ph.51.030189.004233 · Cited by 469
Multiple pathways of cytochrome c release from mitochondria in apoptosis
Gogvadze, V. G., Orrenius, S., & Zhivotovsky, B. (2006) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2006.03.016 · Cited by 467
Nitric oxide in the human respiratory cycle
McMahon, T., Moon, R. E., Luschinger, B. P., Carraway, M. S., Stone, A. E., Stolp, B. W., Gow, A. J., Pawloski, J. R., Watke, P., Singel, D. J., et al. (2002) · Nature Medicine · doi:10.1038/nm718 · Cited by 462
Anaerobic Metabolism in Plants
Kennedy, R., Rumpho, M. E., & Fox, T. C. (1992) · PLANT PHYSIOLOGY · doi:10.1104/pp.100.1.1 · Cited by 461
Flagged first, then by citations
Research works printed but not linked: 138
- Tannenbaum, 1974, J. Cancer Inst., 53, 79
- Bartsch, 1988, Mutat. Res., 202, 307
- Fowler, 2013, Philos. Trans. R. Soc., B, 368, 164
- Boyd, 2013, Front. Microbiol., 4, 201
- Lin, 1997, Adv. Microb. Physiol., 39, 1
- Zumft, 1997, Microbiol. Mol. Biol. Rev., 61, 533
- Lehnert, 2011, The Handbook of Porphyrin Science, 1
- http://www.ncbi.nlm.nih.gov/mesh/68042441.
- Broda, 1977, Z. Allg. Mikrobiol., 17, 491, 10.1002/jobm.19770170611 · DOI
- Shen, 2012, Front. Microbiol., 3, 269
- Ducluzeau, 2009, TIBS, 34, 9
- Lu, 2005, Hepatobiliary Pancreatic Dis. Int., 4, 350
- Tsuchiya, 2005, Am. J. Physiol.: Heart Circ. Physiol., 288, H2163
- Sies, 1991, Oxidative Stress II: Oxidants and Antioxidants
- Frost, 2005, Am. J. Physiol.: Regul., Integr. Comp. Physiol., 288, R394
- Badejo, 2010, Am. J. Physiol.: Heart Circ. Physiol., 299, H819
- Tsai, 2004, Antioxid. Redox Signaling, 6, 1011, 10.1089/ars.2004.6.1011 · DOI
- Bertuglia, 2005, Am. J. Physiol.: Heart Circ. Physiol., 288, H525
- Gladwin, 2006, Am. J. Physiol.: Heart Circ. Physiol., 291, H2026
- Thomas, 2001, Proc. Natl. Acad. Sci. U.S.A., 98, 355, 10.1073/pnas.98.1.355 · DOI · Paper page
- Tsuchiya, 2005, Am. J. Physiol.: Heart Circ. Physiol., 288, H2163
- Hataishi, 2006, Am. J. Physiol.: Heart Circ. Physiol., 291, H379
- Dalsgaard, 2007, Am. J. Physiol.: Heart Circ. Physiol., 292, H3072
- Isbell, 2007, Am. J. Physiol.: Heart Circ. Physiol., 293, H2565
- Minneci, 2008, Am. J. Physiol.: Heart Circ. Physiol., 295, H743
- Dufour, 2010, Am. J. Physiol.: Heart. Circ. Physiol., 299, H1936
- Hopmann, 2011, Chem.─Eur. J., 17, 6348
- Grätzel, 1970, Ber. Bunsen-Ges. Phys. Chem., 74, 488, 10.1002/bbpc.19700740513 · DOI
- Wink, 1993, Chem. Res. Toxicol., 6, 23, 10.1021/tx00031a003 · DOI · Paper page
- Kharitonov, 1995, Biol. Chem., 270, 28158, 10.1074/jbc.270.47.28158 · DOI
- Blood, 2009, Am. J. Physiol.: Heart Circ. Physiol., 296, H237
- Feelisch, 2002, FASEB J., 16, 1775, 10.1096/fj.02-0363com · DOI · Paper page
- Nadra, 2007, Proteins: Struct., Funct., Bioinf., 71, 695, 10.1002/prot.21814 · DOI
- Burmester, 2004, News Physiol. Sci., 19, 110
- Lechauve, 2010, FEBS J., 277, 2696
- Rose, 1983, J. Am. Chem. Soc., 105, 2866, 10.1021/ja00347a056 · DOI
- Hoshino, 1993, J. Am. Chem. Soc., 115, 9568, 10.1021/ja00074a023 · DOI
- Shiva, 2007, J. Exp. Med., 204, 2089, 10.1084/jem.20070198 · DOI · Paper page
- Parks, 1986, Acta Physiol. Scand. Suppl., 548, 87
- Eddy, 1987, Am. J. Physiol., 253, H709
- Sarnesto, 1996, Lab. Invest., 74, 48
- Linder, 1999, Lab. Invest., 79, 967
- Angermuller, 1987, Eur. J. Cell Biol., 45, 137
- Sergeev, 1985, J. Appl. Biochem., 86
- Wu, 2003, Alcohol Res. Health, 27, 277
- Alikulov, 1980, Biokhimiia, 45, 1714
- Williamson, 1977, Pathophysiology and Therapeutics of Myocardial Ischemia, 193
- Roy, 1982, Fed. Proc., 41, 767
- Parks, 1988, Am. J. Physiol., 254, G768
- Lundberg, 2005, Arterioscler., Thromb., Vasc. Biol., 25, 915, 10.1161/01.ATV.0000161048.72004.c2 · DOI · Paper page
- Terada, 1992, Am. J. Physiol., 263, L394
- Friedl, 1990, Am. J. Pathol., 136, 491
- Yokoyama, 1990, Am. J. Physiol., 258, G564
- Weinbroum, 1995, Am. J. Physiol., 268, G988
- Webb, 2008, Hypertension, 51, 784, 10.1161/HYPERTENSIONAHA.107.103523 · DOI · Paper page
- Modin, 2001, Acta Physiol. Scand., 171, 9
- Opie, 1976, Circ. Res., 38, 152
- Li, 2008, J. Biol. Chem., 283, 17855, 10.1074/jbc.M801785200 · DOI · Paper page
- Aamand, 2009, Am. J. Physiol.: Heart Circ. Physiol., 297, H2068
- Nicolis, 2004, Chem.─Eur. J., 10, 2281
- Rodkey, 1976, Clin. Chem., 22, 1986, 10.1093/clinchem/22.12.1986 · DOI
- Herold, 2001, Biochemistry, 40, 3385, 10.1021/bi002407m · DOI · Paper page
- Huang, 2002, Morb. Mortal. Wkly. Rep., 51, 639
- Khoo, 1994, Eur. J. Clin. Chem. Clin. Biochem., 32, 435440
- Liu, 1997, Am. J. Physiol., 272, H2327, 10.1152/ajpcell.1997.272.6.C1919 · DOI
- Casella, 2006, Chem.─Eur. J., 12, 749
- Anni, 1992, Met. Ions Biol. Syst., 28, 219
- Dunford, 1999, Heme Peroxidases
- Reszka, 2012, Am. J. Physiol.: Lung Cell. Mol. Physiol., 302, L1044
- Castro, 2004, Arch. Biochem. Biophys., 421, 99, 10.1016/j.abb.2003.08.033 · DOI · Paper page
- Roberg, 1998, Am. J. Pathol., 152, 1151
- Vitturi, 2009, Am. J. Physiol.: Heart Circ. Physiol., 296, H1398
- Jensen, 2010, Am. J. Physiol.: Regul., Integr. Comp. Physiol., 298, R972
- Lefer, 2006, Am. J. Physiol.: Renal Physiol., 290, F777
- Casey, 2009, Am. J. Physiol.: Heart Circ. Physiol., 296, H524
- Ingram, 2010, Am. J. Physiol.: Heart Circ. Physiol., 298, H331
- Nossaman, 2010, Asian J. Exp. Biol. Sci, 1, 451
- Lundberg, 2011, Cardiovasc. Res., 89, 525, 10.1093/cvr/cvq325 · DOI · Paper page
- Gould, 2003, Free Radical Res., 37, 38
- Trapido-Rosenthal, 2001, Am. Zool., 41, 247
- Crawford, 1995, Plant Cell, 7, 859
- Magalhaes, 2002, Physiol. Mol. Biol. Plants, 8, 11
- Ricard, 1994, Plant Physiol. Biochem., 32, 1
- Liao, 1994, Plant Physiol. Biochem., 32, 479
- Fan, 1997, J. Exp. Bot., 48, 1655
- Botrel, 1996, Plant Physiol. Biochem., 34, 645
- Kaiser, 1999, Physiol. Plant., 105, 385, 10.1034/j.1399-3054.1999.105225.x · DOI
- Lager, 2010, Plant, Cell Environ., 33, 1513
- Bashford, 1987, J. Mol. Biol., 196, 199, 10.1016/0022-2836(87)90521-3 · DOI
- Weiland, 2004, J. Am. Chem. Soc., 126, 11930, 10.1021/ja046990w · DOI
- Nadra, 2008, Proteins, 71, 695, 10.1002/prot.21814 · DOI
- Hargrove, 2000, Structure, 8, 1005, 10.1016/S0969-2126(00)00194-5 · DOI
- Hoy, 2007, J. Mol. Biol., 371, 168, 10.1016/j.jmb.2007.05.029 · DOI
- Hill, 1998, Can. J. Bot., 76, 707
- Smagghe, 2006, Biochemistry, 45, 561, 10.1021/bi051902l · DOI
- Trent, 2001, J. Biol. Chem., 276, 30106, 10.1074/jbc.C100300200 · DOI
- Trent, 2002, J. Biol. Chem., 277, 19538, 10.1074/jbc.M201934200 · DOI
- Ward, 1988, Plant Physiol., 88, 1144, 10.1104/pp.88.4.1141 · DOI
- Prioul, 1985, Physiol. Veg., 23, 175
- Colter, 1950, Arch. Biochem., 27, 368
- del Rio, 2011, Arch. Biochem. Biophys., 506, 1, 10.1016/j.abb.2010.10.022 · DOI
- Benamar, 2008, Biochim. Biophys. Acta, 1777, 1268, 10.1016/j.bbabio.2008.06.002 · DOI
- Stachura, 1996, J. Physiol. Pharmacol., 47, 131
- Bird, 2002, Structure, 10, 168, 10.1016/S0969-2126(02)00911-5 · DOI
- Calmels, 1988, J. Gen. Microbiol., 134, 221
- Couture, 2000, Eur. J. Biochem., 267, 4770, 10.1046/j.1432-1327.2000.01531.x · DOI
- Li, 2001, Handbook of Metalloproteins, 486
- Rosenfeld, 2001, Handbook of Metalloproteins, 285
- Gajhede, 2001, Handbook of Metalloproteins, 195
- Mate, 2001, Handbook of Metalloproteins, 486
- Malkin, 1970, Adv. Enzymol., 33, 177
- Vanngard, 1972, Biological Applications of Electron Spin Resonance, 411
- Silveira, 2010, Bioinorg. Chem. Appl.
- Vine, 2011, Biochem. Soc. Trans., 39, 213, 10.1042/BST0390213 · DOI
- Flores, 2005, Photosynth. Res., 83, 117, 10.1007/s11120-004-5830-9 · DOI
- Gates, 2011, Biochem. J., 435, 743, 10.1042/BJ20101920 · DOI
- Hase, 2006, Photosystem 1, 477, 10.1007/978-1-4020-4256-0_28 · DOI
- Hewitt, 1975, Annu. Rev. Plant Physiol., 26, 73, 10.1146/annurev.pp.26.060175.000445 · DOI
- Knaff, 1991, Biochim. Biophys. Acta, 1056, 93, 10.1016/S0005-2728(05)80277-4 · DOI
- Kartal, 2011, Nature, 479, 127, 10.1038/nature10453 · DOI
- Williams, 1995, Nat. Struct. Biol., 2, 975, 10.1038/nsb1195-975 · DOI
- Ranghino, 2000, Biochemistry, 39, 10958, 10.1021/bi000178y · DOI
- Suzuki, 1994, J. Am. Chem. Soc., 116, 11154
- Iwasaki, 1972, J. Biochem., 71, 645
- Grazina, 2013, Bioinorganic Fundamentals and Applications: Metals in Natural Living Systems and Metals in Toxicology and Medicine, 103
- Massey, 1969, J. Biol. Chem., 244, 1682, 10.1016/S0021-9258(18)91738-2 · DOI
- Olson, 1974, J. Biol. Chem., 249, 4350, 10.1016/S0021-9258(19)42427-7 · DOI
- Stirpe, 1969, J. Biol. Chem., 244, 3855, 10.1016/S0021-9258(17)36428-1 · DOI
- Waud, 1976, Arch. Biochem. Biophys., 172, 354, 10.1016/0003-9861(76)90087-4 · DOI
- Waud, 1976, Arch. Biochem. Biophys., 172, 365, 10.1016/0003-9861(76)90088-6 · DOI
- Harris, 1997, J. Biol. Chem., 272, 8370, 10.1074/jbc.272.13.8370 · DOI · Paper page
- Hearse, 1986, Acta Physiol. Scand., 548, 65
- Granger, 1986, Acta Physiol. Scand., 548, 47
- Fabre, 1986, Biochem. Pharmacol., 35, 1325, 10.1016/0006-2952(86)90277-7 · DOI
- Kumar, 2011, Expert Opin. Ther. Pat., 211071
- van de Vossenberg, 2013, Environ. Microbiol., 15, 1275, 10.1111/j.1462-2920.2012.02774.x · DOI
- Kroneck, 2002, Met. Ions Biol. Syst., 39, 369
- Krüger, 1987, FEMS Microbiol. Lett., 48, 225, 10.1016/0378-1097(87)90166-2 · DOI
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Metadata
- Authors
- Maia, L. B., & Moura, J. J. G.
- Affiliations
- Universidade Nova de Lisboa , , ,
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 2014-04-02
- Volume
- 114
- Issue
- 10
- Pages
- 5273-5357
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- OpenAlex
- W2332921714
- Cited by
- 401
- References
- 1,549
- Citations by year
- 2026: 34 · 2025: 66 · 2024: 50 · 2023: 41 · 2022: 41 · 2021: 41 · 2020: 23 · 2019: 24 · 2018: 24 · 2017: 12 · 2016: 22 · 2015: 13 · 2014: 10
- FWCI
- 2.23
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- Chemical Reviews (publishedVersion, other-oa)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- Physical Sciences › Environmental Science › Pollution › Wastewater Treatment and Nitrogen Removal
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Metalloenzymes and iron-sulfur proteins
- Keywords
- nitrite, nitrite metabolism, nitrite reduction, nitrite oxidation, nitrite reductase, bioinorganic chemistry, redox reactions, nitric oxide
- MeSH terms
- Animals, Bacteria, Humans, Nitrites, Nitrogen, Oxidation-Reduction, Plants, Signal Transduction, Ammonium Compounds
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