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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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Items 1,201–1,400 of 1,549
Myoglobin-Catalyzed Tyrosine Nitration: No Need for Peroxynitrite
Kılınç, K., Kılınç, A., Wolf, R. E., & Grisham, M. B. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5168 · Cited by 50
Bocahut, A., Bernad, S., Sebban, P., & Sacquin‐Mora, S. (2009) · The Journal of Physical Chemistry B · doi:10.1021/jp906854x · Cited by 50
Horchani, F., Aschi‐Smiti, S., & Brouquisse, R. (2010) · Acta Physiologiae Plantarum · doi:10.1007/s11738-010-0503-0 · Cited by 50
Nasri, H., Ellison, M. K., Shang, M., Schulz, C. E., & Scheidt, W. R. (2004) · Inorganic Chemistry · doi:10.1021/ic035119y · Cited by 50
Brondino, C. D., Rivas, M. G., Romão, M. J., Moura, J. J. G., & Moura, I. (2006) · Accounts of Chemical Research · doi:10.1021/ar050104k · Cited by 50
Self-citationCovalent crosslinking of the heme prosthetic group to myoglobin by H2O2: Toxicological implications
Osawa, Y., & Williams, M. S. (1996) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(95)02215-5 · Cited by 50
Correlations between Structure and Spectroscopic Properties in Membrane Model System
Letellìer, L., & Shechter, E. (1973) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1973.tb03220.x · Cited by 49
Cell signaling mediated by nitrated cyclic guanine nucleotide
Akaike, T., Fujii, S., Sawa, T., & Ihara, H. (2010) · Nitric Oxide · doi:10.1016/j.niox.2010.06.006 · Cited by 49
Maia, L. B., Duarte, R. O., Freire, A. P., Moura, J. J. G., & Mira, L. (2007) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-007-0229-7 · Cited by 49
Self-citationNitrosative stress in Escherichia coli: reduction of nitric oxide
Vine, C. E., & Cole, J. A. (2011) · Biochemical Society Transactions · doi:10.1042/bst0390213 · Cited by 49
Bonner, F. T., & Pearsall, K. A. (1982) · Inorganic Chemistry · doi:10.1021/ic00135a053 · Cited by 49
Wang, J., & Wu, J. (2004) · Nitric Oxide · doi:10.1016/j.niox.2004.10.003 · Cited by 49
Kitatsuji, C., Kurogochi, M., Nishimura, S., Ishimori, K., & Wakasugi, K. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.02.002 · Cited by 49
Kostera, J., Youngblut, M. D., Slosarczyk, J. M., & Pacheco, A. A. (2008) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-008-0393-4 · Cited by 48
Neuroglobin ligand binding kinetics
Kiger, L., Uzan, J., Dewilde, S., Burmester, T., Hankeln, T., Moens, L., Hamdane, D., Baudin‐Creuza, V., & Marden, M. C. (2004) · IUBMB Life · doi:10.1080/15216540500037711 · Cited by 48
Circulating nitrite anions are a directly acting vasodilator and are donors for nitric oxide
DEMONCHEAUX, E. A. G., HIGENBOTTAM, T. W., FOSTER, P. J., BORLAND, C. D. R., SMITH, A. P. L., MARRIOTT, H. M., BEE, D., AKAMINE, S., & DAVIES, M. B. (2002) · Clinical Science · doi:10.1042/cs1020077 · Cited by 48
Nasri, H., Wang, Y., Huynh, B. H., Walker, F. A., & Scheidt, W. R. (1991) · Inorganic Chemistry · doi:10.1021/ic00007a012 · Cited by 48
Salhany, J. M. (2008) · Biochemistry · doi:10.1021/bi8000819 · Cited by 48
Shiva, S., Rassaf, T., Patel, R. P., & Gladwin, M. T. (2010) · Cardiovascular Research · doi:10.1093/cvr/cvq327 · Cited by 48
Koppenhöfer, A., Turner, K. L., Allen, J. W. A., Chapman, S. K., & Ferguson, S. J. (2000) · Biochemistry · doi:10.1021/bi000192a · Cited by 48
Physiological and phylogenetic study of an ammonium-oxidizing culture at high nitrite concentrations
Tan, N. C. G., Kampschreur, M. J., Wanders, W., van der Pol, W. L. J., van de Vossenberg, J. L. C. M., Kleerebezem, R., van Loosdrecht, M. C. M., & Jetten, M. S. M. (2008) · Systematic and Applied Microbiology · doi:10.1016/j.syapm.2008.01.002 · Cited by 48
Divergent distribution of cytoglobin and neuroglobin in the murine eye
Schmidt, M., Laufs, T., Reuss, S., Hankeln, T., & Burmester, T. (2004) · Neuroscience Letters · doi:10.1016/j.neulet.2004.10.071 · Cited by 48
EPR−ENDOR of the Cu(I)NO Complex of Nitrite Reductase
Usov, O. M., Sun, Y., Grigoryants, V. M., Shapleigh, J. P., & Scholes, C. P. (2006) · Journal of the American Chemical Society · doi:10.1021/ja056166n · Cited by 48
Possible Neuroprotective Mechanism of Human Neuroglobin
Wakasugi, K., Kitatsuji, C., & Morishima, I. (2005) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2005.tb00028.x · Cited by 48
Diurnal changes in nitrogen assimilation of tobacco roots
Stöhr, C., & Mäck, G. (2001) · Journal of Experimental Botany · doi:10.1093/jexbot/52.359.1283 · Cited by 47
Wakasugi, K., & Morishima, I. (2005) · Biochemistry · doi:10.1021/bi0477539 · Cited by 47
Hybrid Respiration in the Denitrifying Mitochondria of Fusarium oxysporum
Takaya, N. (2003) · The Journal of Biochemistry · doi:10.1093/jb/mvg060 · Cited by 47
Effect of culture P o 2on macrophage (RAW 264.7) nitric oxide production
Otto, C. M., & Baumgardner, J. E. (2001) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.2001.280.2.c280 · Cited by 47
Tissue acidosis in myocardial hypoxia
Cobbe, S. M. (1980) · Journal of Molecular and Cellular Cardiology · doi:10.1016/0022-2828(80)90078-4 · Cited by 47
Electronic Structure Description of thecis-MoOS Unit in Models for Molybdenum Hydroxylases
Doonan, C. J., Rubie, N. D., Peariso, K., Harris, H. H., Knottenbelt, S. Z., George, G. N., Young, C. G., & Kirk, M. L. (2007) · Journal of the American Chemical Society · doi:10.1021/ja068512m · Cited by 47
Pinheiro, T. J. T., Cheng, H., Seeholzer, S. H., & Röder, H. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.4159 · Cited by 47
Coupling of the heme and an internal disulfide bond in human neuroglobin
Hamdane, D., Kiger, L., Dewilde, S., Green, B. N., Pesce, A., Uzan, J., Burmester, T., Hankeln, T., Bolognesi, M., Moens, L., et al. (2004) · Micron · doi:10.1016/j.micron.2003.10.019 · Cited by 47
Simon, J., Kern, M., Hermann, B. A., Einsle, O., & Butt, J. N. (2011) · Biochemical Society Transactions · doi:10.1042/bst20110713 · Cited by 47
Kim, D., Yamaguchi, K., & Oda, T. (2006) · Journal of Plankton Research · doi:10.1093/plankt/fbi145 · Cited by 47
Rodríguez-Roldán, V., García-Heredia, J. M., Navarro, J. A., la Rosa, M. Á. D., & Hervás, M. (2008) · Biochemistry · doi:10.1021/bi801329s · Cited by 47
Oliveira, T. F., Franklin, E., Afonso, J. P., Khan, A. R., Oldham, N. J., Pereira, I. A. C., & Archer, M. (2011) · Frontiers in Microbiology · doi:10.3389/fmicb.2011.00071 · Cited by 46
Hendgen-Cotta, U. B., Kelm, M., & Rassaf, T. (2010) · Nitric Oxide · doi:10.1016/j.niox.2009.10.003 · Cited by 46
Purification and characterization of a chlorite dismutase fromPseudomonas chloritidismutans
Mehboob, F., Wolterink, A., Vermeulen, A. J., Jiang, B., Hagedoorn, P., Stams, A. J. M., & Kengen, S. W. M. (2009) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2009.01517.x · Cited by 46
Magnetic resonance study of the transmembrane nitrite diffusion
Samouilov, A., Woldman, Y. Y., Zweier, J. L., & Khramtsov, V. V. (2007) · Nitric Oxide · doi:10.1016/j.niox.2006.12.006 · Cited by 46
Ali, H. I., Fujita, T., Akaho, E., & Nagamatsu, T. (2009) · Journal of Computer-Aided Molecular Design · doi:10.1007/s10822-009-9314-z · Cited by 46
Nitric Oxide Regulates Shikonin Formation in Suspension-Cultured Onosma paniculatum Cells
Wu, S.-J., Qi, J.-L., Zhang, W.-J., Liu, S.-H., Xiao, F. H., Zhang, M.-S., Xu, G., Zhao, W., Shi, M.-W., Pang, Y.-J., et al. (2008) · Plant and Cell Physiology · doi:10.1093/pcp/pcn178 · Cited by 46
Hemoglobin can nitrate itself and other proteins
Grzelak, A., Balcerczyk, A., Mateja, A., & Bartosz, G. (2001) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/s0304-4165(01)00176-3 · Cited by 45
A switch in heme axial ligation prepares Paracoccus pantotrophus cytochrome cd1 for catalysis.
Watmough, N. J., Ferguson, S. J., & Allen, J. W. A. (2000) · Nature Structural Biology · doi:10.1038/82821 · Cited by 45
Autocatalytic Oxidation of Hemoglobin by Nitrite: A Possible Mechanism
Lissi, E. A. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(98)00004-5 · Cited by 45
Neuroprotection and the role of neuroglobin
Garry, D. J., & Mammen, P. P. A. (2003) · The Lancet · doi:10.1016/s0140-6736(03)14055-x · Cited by 45
Bykov, D., & Neese, F. (2012) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-012-0893-0 · Cited by 45
Fast Dissociation of Nitric Oxide from Ferrous Pseudomonas aeruginosa cd1 Nitrite Reductase
Rinaldo, S., Arcovito, A., Brunori, M., & Cutruzzolà, F. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700933200 · Cited by 45
Stable Copper−Nitrosyl Formation by Nitrite Reductase in Either Oxidation State
Tocheva, E. I., Rosell, F. I., Mauk, A. G., & Murphy, M. E. P. (2007) · Biochemistry · doi:10.1021/bi701205j · Cited by 45
Rates of nitric oxide dissociation from hemoglobin
Azizi, F., Kielbasa, J. E., Adeyiga, A. M., Maree, R. D., Frazier, M., Yakubu, M., Shields, H. W., King, S. B., & Kim‐Shapiro, D. B. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.03.001 · Cited by 44
Theoretical insight into the hydroxylamine oxidoreductase mechanism
Fernández, M. L., Estrin, D. A., & Bari, S. E. (2008) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2008.01.032 · Cited by 44
Involvement of chloroplast and mitochondria redox valves in nitrate assimilation
Quesada, A., Gómez-Garcı́a, I., & Fernández, E. M. (2000) · Trends in Plant Science · doi:10.1016/s1360-1385(00)01770-2 · Cited by 44
Pattillo, C. B., Bir, S. C., Rajaram, V., & Kevil, C. G. (2010) · Cardiovascular Research · doi:10.1093/cvr/cvq297 · Cited by 44
Functional Expression of Two Arabidopsis Aldehyde Oxidases in the Yeast Pichia pastoris
Koiwai, H., Akaba, S., Seo, M., Komano, T., & Koshiba, T. (2000) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a022654 · Cited by 44
Lin, P., Kreutzer, U., & Jue, T. (2007) · Biophysical Journal · doi:10.1529/biophysj.106.094458 · Cited by 44
Hsieh, Y., Liu, M., Wang, V. C. ‐., Chiang, Y. L., Liu, E., Wu, W.-G., Chan, S. I., & Chen, C. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07390.x · Cited by 44
Shingles, R., Roh, M. H., & McCarty, R. E. (1997) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1022491220299 · Cited by 43
Iwaasa, H., Takagi, T., & Shikama, K. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38930-6 · Cited by 43
Badwey, J. A., Robinson, J. M., Karnovsky, M. J., & Karnovsky, M. J. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)69634-1 · Cited by 43
Maia, L. B., & Mira, L. (2002) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2002.2781 · Cited by 43
Self-citationThe electrochemical reduction of iron porphyrin nitrosyls in the presence of weak acids
Liu, Y., & Ryan, M. D. (1994) · Journal of Electroanalytical Chemistry · doi:10.1016/0022-0728(93)03101-t · Cited by 43
Aldehyde oxidase and xanthine oxidase-functional and evolutionary relationships
Krenitsky, T. A. (1978) · Biochemical Pharmacology · doi:10.1016/0006-2952(78)90186-7 · Cited by 43
Ranghino, G., Scorza, E., Sjögren, T., Williams, P. A., Ricci, M., & Hajdu, J. (2000) · Biochemistry · doi:10.1021/bi000178y · Cited by 43
Bykov, D., & Neese, F. (2010) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-010-0739-6 · Cited by 43
Low NO Concentration Dependence of Reductive Nitrosylation Reaction of Hemoglobin
Tejero, J., Basu, S., Helms, C. C., Hogg, N., King, S. B., Kim‐Shapiro, D. B., & Gladwin, M. T. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.298927 · Cited by 43
Knipp, M., & He, C. (2011) · IUBMB Life · doi:10.1002/iub.451 · Cited by 43
In quest of the nitrogen oxidizing prokaryotes of the early Earth
Vlaeminck, S. E., Hay, A. G., Maignien, L., & Verstraete, W. (2010) · Environmental Microbiology · doi:10.1111/j.1462-2920.2010.02345.x · Cited by 43
Human xanthine oxidoreductase: in search of a function
Harrison, R. (1997) · Biochemical Society Transactions · doi:10.1042/bst0250786 · Cited by 43
Makino, M., Sugimoto, H., Sawai, H., Kawada, N., Yoshizato, K., & Shiro, Y. (2006) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444906013813 · Cited by 43
Degradation of chlorophyll by nitrogen dioxide generated from nitrite by the peroxidase reaction
Shibata, H., Kono, Y., Yamashita, S., Sawa, Y., Ochiai, H., & Tanaka, K. (1995) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(95)00031-d · Cited by 43
In Vitro Killing of Mycobacterium ulcerans by Acidified Nitrite
Phillips, R., Kuijper, S., Benjamin, N., Wansbrough-Jones, M., Wilks, M., & Kolk, A. H. J. (2004) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.48.8.3130-3132.2004 · Cited by 43
Hydroxylamine Reduction to Ammonium by Plant and Cyanobacterial Hemoglobins
Sturms, R., DiSpirito, A. A., Fulton, D. B., & Hargrove, M. S. (2011) · Biochemistry · doi:10.1021/bi201425f · Cited by 43
Pisa, R., Stein, T. H., Eichler, R., Groß, R., & Simon, J. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.02784.x · Cited by 42
Cytochrome c Mutants for Superoxide Biosensors
Wegerich, F., Turano, P., Allegrozzi, M., Möhwald, H., & Lisdat, F. (2009) · Analytical Chemistry · doi:10.1021/ac802571h · Cited by 42
Merkle, A. C., & Lehnert, N. (2009) · Inorganic Chemistry · doi:10.1021/ic9018376 · Cited by 42
Structural and functional properties of class 1 plant hemoglobins
Igamberdiev, A. U., Bykova, N. V., & Hill, R. D. (2011) · IUBMB Life · doi:10.1002/iub.439 · Cited by 42
Hemoglobin as a Nitrite Anhydrase: Modeling Methemoglobin‐Mediated N2O3 Formation
Hopmann, K. H., Cardey, B., Gladwin, M. T., Kim‐Shapiro, D. B., & Ghosh, A. (2011) · Chemistry - A European Journal · doi:10.1002/chem.201003578 · Cited by 42
Characterization of A New Copper(I)−Nitrito Complex That Evolves Nitric Oxide
Chuang, W., Lin, I.-J., Chen, H., Chang, Y., & Hsu, S. C. N. (2010) · Inorganic Chemistry · doi:10.1021/ic100083b · Cited by 42
Study of the hypoxia-dependent regulation of human CYGB gene
Guo, X., Philipsen, S., & Tan-Un, K. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.09.108 · Cited by 42
Ellis, M. J., Prudêncio, M., Dodd, F. E., Strange, R. W., Sawers, R. G., Eady, R. R., & Hasnain, S. S. (2002) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5304 · Cited by 42
Lespade, L., & Bercion, S. (2009) · The Journal of Physical Chemistry B · doi:10.1021/jp9041809 · Cited by 42
Hirasawa, M., Fukushima, K., Tamura, G., & Knaff, D. B. (1984) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(84)90004-9 · Cited by 42
Immunohistochemical Determination of Cytosolic Cytochrome c Concentration in Cardiomyocytes
van Beek-Harmsen, B. J., & van der Laarse, W. J. (2005) · Journal of Histochemistry & Cytochemistry · doi:10.1369/jhc.4c6527.2005 · Cited by 42
Hirasawa, M., Tripathy, J. N., Sommer, F., Ramasamy, S., Chung, J. S., Nestander, M. A., Kruthiventi, M., Zabet‐Moghaddam, M., Johnson, M. K., Merchant, S., et al. (2009) · Photosynthesis Research · doi:10.1007/s11120-009-9512-5 · Cited by 42
Hormonal Regulation of Organic and Phosphoric Acid Release by Barley Aleurone Layers and Scutella
Drozdowicz, Y. M., & Jones, R. L. (1995) · PLANT PHYSIOLOGY · doi:10.1104/pp.108.2.769 · Cited by 41
Transient kinetic and oxidation-reduction studies of spinach ferrodoxin: nitrate oxidoreductase
Hirasawa, M., Tollin, G., Salamon, Z., & Knaff, D. B. (1994) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(94)90249-6 · Cited by 41
Calcineurin Activates Cytoglobin Transcription in Hypoxic Myocytes
Singh, S., Manda, S. M., Sikder, D. S., Birrer, M. J., Rothermel, B. A., Garry, D. J., & Mammen, P. P. A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809572200 · Cited by 41
Wach, M. J., Kers, J. A., Krasnoff, S. B., Loria, R., & Gibson, D. M. (2004) · Nitric Oxide · doi:10.1016/j.niox.2004.11.004 · Cited by 41
Montalbini, P. (1992) · Plant Science · doi:10.1016/0168-9452(92)90154-e · Cited by 41
Inhibition of Nitrite Reduction with Photosynthetic Inhibitors
Klepper, L. A. (1975) · Weed Science · doi:10.1017/s0043174500052826 · Cited by 41
Nitrite Reduces Acute Lung Injury and Improves Survival in a Rat Lung Transplantation Model
Sugimoto, R., Okamoto, T., Nakao, A., Zhan, J., Wang, Y., Kohmoto, J., Tokita, D., Farver, C. F., Tarpey, M. M., Billiar, T. R., et al. (2012) · American Journal of Transplantation · doi:10.1111/j.1600-6143.2012.04169.x · Cited by 40
Cutruzzolà, F., Arese, M., Grasso, S., Bellelli, A., & Brunori, M. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00583-8 · Cited by 40
Clarke, T. A., Kemp, G. L., Wonderen, J. H. V., Doyle, R.-M. A. S., Cole, J. A., Tovell, N., Cheesman, M. R., Butt, J. N., Richardson, D. J., & Hemmings, A. M. (2008) · Biochemistry · doi:10.1021/bi702175w · Cited by 40
Reece, S. Y., Woodward, J. J., & Marletta, M. A. (2009) · Biochemistry · doi:10.1021/bi900385g · Cited by 40
Bocahut, A., Derrien, V., Bernad, S., Sebban, P., Sacquin‐Mora, S., Guittet, É., & Lescop, E. (2012) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-012-0956-2 · Cited by 40
Boulanger, M. J., & Murphy, M. E. P. (2003) · Protein Science · doi:10.1110/ps.0224503 · Cited by 40
Smart, D. R., Ritchie, K., Bloom, A. J., & Bugbee, B. G. (1998) · Plant Cell & Environment · doi:10.1046/j.1365-3040.1998.00315.x · Cited by 40
Enzymatic Interconversion of Ammonia and Nitrite: The Right Tool for the Job
Kostera, J., McGarry, J. M., & Pacheco, A. A. (2010) · Biochemistry · doi:10.1021/bi1006783 · Cited by 40
Fülöp, V., Watmough, N. J., & Ferguson, S. J. (2000) · Advances in inorganic chemistry · doi:10.1016/s0898-8838(00)51003-4 · Cited by 39
Mechanism of nitrite‐stimulated catalysis by lactoperoxidase
Brück, T., Fielding, R. J., Symons, M. C. R., & Harvey, P. J. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2001.02213.x · Cited by 39
Nitrite Reductase Activity of Sol-Gel-encapsulated Deoxyhemoglobin
Roche, C. J., Dantsker, D., Samuni, U., & Friedman, J. M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603914200 · Cited by 39
Spectroscopic Characterization of the NO Adduct of Hydroxylamine Oxidoreductase
Hendrich, M. P., Upadhyay, A. K., Riga, J. M., Arciero, D. M., & Hooper, A. B. (2002) · Biochemistry · doi:10.1021/bi011332z · Cited by 39
Kozlov, A. V., Costantino, G., Sobhian, B., Szalay, L., Umar, F., Nohl, H., Bahrami, S., & Redl, H. R. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.515 · Cited by 39
Kuznetsova, S. A., Knaff, D. B., Hirasawa, M., Lagoutte, B., & Setif, P. Q. Y. (2003) · Biochemistry · doi:10.1021/bi035662q · Cited by 39
Structural Dynamics of Myoglobin: FTIR-TDS Study of NO Migration and Binding†
Nienhaus, K., Palladino, P., & Nienhaus, G. U. (2007) · Biochemistry · doi:10.1021/bi701935v · Cited by 39
Interaction of ferredoxin-linked nitrite reductase with ferredoxin
Hirasawa, M., & Knaff, D. B. (1985) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(85)90025-1 · Cited by 39
Nitric Oxide and Cnidarian-Dinoflagellate Symbioses: Pieces of a Puzzle
Trapido‐Rosenthal, H. G., Sharp, K. H., Galloway, T. S., & Morrall, C. E. (2001) · American Zoologist · doi:10.1093/icb/41.2.247 · Cited by 39
Kinetic studies on the oxidation of phenols by the horseradish peroxidase compound II
Patel, P. K., Mondal, M. S., Modi, S. P., & Behere, D. V. (1997) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(96)00219-1 · Cited by 38
Bab-Dinitz, E., Shmuely, H., Maupin-furlow, J. A., Eichler, J., & Shaanan, B. (2006) · Bioinformatics · doi:10.1093/bioinformatics/btk043 · Cited by 38
The Sixteenth Iron in the Nitrogenase MoFe Protein
Zhang, L., Kaiser, J. T., Meloni, G., Yang, K., Spatzal, T., Andrade, S. L. A., Einsle, O., Howard, J. B., & Rees, D. C. (2013) · Angewandte Chemie International Edition · doi:10.1002/anie.201303877 · Cited by 38
Radoul, M., Bykov, D., Rinaldo, S., Cutruzzolà, F., Neese, F., & Goldfarb, D. (2011) · Journal of the American Chemical Society · doi:10.1021/ja109688w · Cited by 38
Bursakov, S. A., Gavel, O. Y., Rocco, G. D., Lampreia, J., Calvete, J. J., Pereira, A. S., Moura, J. J. G., & Moura, I. (2003) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2003.12.002 · Cited by 38
Self-citationDey, S. G., Dey, A., Usov, O. M., Sun, Y., Grigoryants, V. M., Scholes, C. P., & Solomon, E. I. (2007) · Journal of the American Chemical Society · doi:10.1021/ja072841c · Cited by 38
Easy Oxidation and Nitration of Human Myoglobin by Nitrite and Hydrogen Peroxide
Nicolis, S., Pennati, A., Perani, E., Monzani, E., Sanangelantoni, A. M., & Casella, L. (2005) · Chemistry - A European Journal · doi:10.1002/chem.200500361 · Cited by 38
Krzemiński, Ł., Ndamba, L. A., Canters, G. W., Aartsma, T. J., Evans, S. D., & Jeuken, L. J. C. (2011) · Journal of the American Chemical Society · doi:10.1021/ja204891v · Cited by 38
Formation of Ferrihæmoglobin of Isolated Human Hæmoglobin Types by Sodium Nitrite
MARTIN, H., & Huisman, T. H. J. (1963) · Nature · doi:10.1038/200898a0 · Cited by 38
Nitrate Assimilation in Bacteria
Moreno‐Vivián, C., & Flores, E. (2007) · Elsevier eBooks · doi:10.1016/b978-044452857-5.50018-7 · Cited by 38
Hucklesby, D. P., & Hewitt, E. J. (1970) · Biochemical Journal · doi:10.1042/bj1190615 · Cited by 37
Dodsworth, J. A., Hungate, B. A., de la Torre, J. R., Jiang, H., & Hedlund, B. P. (2010) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-381294-0.00008-0 · Cited by 37
Ligand Migration between Internal Docking Sites in Photodissociated Carbonmonoxy Neuroglobin
Lutz, S., Nienhaus, K., Nienhaus, G. U., & Meuwly, M. (2009) · The Journal of Physical Chemistry B · doi:10.1021/jp905673p · Cited by 37
Beretta, M., Bouwman, E., Casella, L., Douziech, B., Driessen, W. L., Gutierrez-Soto, L., Monzani, E., & Reedijk, J. (2000) · Inorganica Chimica Acta · doi:10.1016/s0020-1693(00)00271-1 · Cited by 37
de Almeida, N. M., Maalcke, W. J., Keltjens, J. T., Jetten, M. S. M., & Kartal, B. (2011) · Biochemical Society Transactions · doi:10.1042/bst0390303 · Cited by 37
Yamaguchi, K., Kataoka, K., Kobayashi, M., Itoh, K., Fukui, A., & Suzuki, S. (2004) · Biochemistry · doi:10.1021/bi0492657 · Cited by 37
Sinha, S. S., Shiva, S., & Gladwin, M. T. (2008) · Trends in Cardiovascular Medicine · doi:10.1016/j.tcm.2008.05.001 · Cited by 37
Role of ATP in nitrite reduction in roots of wheat and pea
Dry, I. B., Wallace, W., & Nicholas, D. J. D. (1981) · Planta · doi:10.1007/bf00385149 · Cited by 37
Enhanced Lipid Oxidation by Oxidatively Modified Myoglobin: Role of Protein-Bound Heme
Vuletich, J. L., Osawa, Y., & Aviram, M. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.2349 · Cited by 37
Lardinois, O. M., & de Montellano, P. R. O. (2004) · Biochemistry · doi:10.1021/bi036241b · Cited by 37
Blood, A. B., Schroeder, H. J., Terry, M. H., Merrill-Henry, J., Bragg, S. L., Vrancken, K., Liu, T., Herring, J. L., Sowers, L. C., Wilson, S. M., et al. (2011) · Circulation · doi:10.1161/circulationaha.110.001073 · Cited by 36
Vine, C. E., Purewal, S. K., & Cole, J. A. (2011) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2011.02385.x · Cited by 36
Formation of Nitric Oxide from Nitrite by the Ferriheme b Protein Nitrophorin 7
He, C., & Knipp, M. (2009) · Journal of the American Chemical Society · doi:10.1021/ja9040362 · Cited by 36
Lopes, H., Besson, S., Moura, I., & Moura, J. J. G. (2001) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s007750000159 · Cited by 36
Self-citationTwo-Dimensional Structure of Membrane-Bound Nitrite Oxidoreductase fromNitrobacter hamburgensis
Spieck, E., Müller, S., Engel, A. H., Mandelkow�, E., Patel, H., & Bock, E. (1996) · Journal of Structural Biology · doi:10.1006/jsbi.1996.0076 · Cited by 36
The assimilatory nitrate reduction system of the phototrophic bacterium Rhodobacter capsulatus E1F1
Pino, C., Olmo-Mira, F., Cabello, P., Martínez‐Luque, M., Castillo, F. J., Roldán, M. D., & Moreno‐Vivián, C. (2006) · Biochemical Society Transactions · doi:10.1042/bst0340127 · Cited by 36
Leferink, N. G. H., Pudney, C. R., Brenner, S., Heyes, D. J., Eady, R. R., Hasnain, S. S., Hay, S., Rigby, S. E. J., & Scrutton, N. S. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.07.003 · Cited by 36
Inhibitory effects of flavonoids on molybdenum hydroxylases activity
Rashidi, M., & Nazemiyeh, H. (2010) · Expert Opinion on Drug Metabolism & Toxicology · doi:10.1517/17425250903426164 · Cited by 36
Xanthine dehydrogenase is transported to the Drosophila eye.
Reaume, A. G., Clark, S. H., & Chovnick, A. (1989) · Genetics · doi:10.1093/genetics/123.3.503 · Cited by 36
Vickers, S. M., Schiller, H. J., Hildreth, J. E. K., & Bulkley, G. B. (1998) · PubMed · Cited by 35
Samal, A. A., Honavar, J., Brandon, A. P., Bradley, K. M., Doran, S. F., Liu, Y., Dunaway, C. W., Steele, C. H., Postlethwait, E. M., Squadrito, G. L., et al. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.08.007 · Cited by 35
Montalbini, P. (1992) · Journal of Phytopathology · doi:10.1111/j.1439-0434.1992.tb01230.x · Cited by 35
Datta, D. B., Triplett, E. W., & Newcomb, E. H. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.11.4700 · Cited by 35
Kemp, G. L., Clarke, T. A., Marritt, S. J., Lockwood, C. W. J., Poock, S. R., Hemmings, A. M., Richardson, D. J., Cheesman, M. R., & Butt, J. N. (2010) · Biochemical Journal · doi:10.1042/bj20100866 · Cited by 35
Cobley, J. G. (1976) · Biochemical Journal · doi:10.1042/bj1560493 · Cited by 35
Molecular Insights into the Functional Role of Myoglobin
Garry, D. J., & Mammen, P. P. A. (2007) · Advances in experimental medicine and biology · doi:10.1007/978-0-387-75434-5_14 · Cited by 34
Reductive nitrosylation and peroxynitrite‐mediated oxidation of heme–hemopexin
Ascenzi, P., Bocedi, A., Antonini, G., Bolognesi, M., & Fasano, M. (2006) · FEBS Journal · doi:10.1111/j.1742-4658.2006.05609.x · Cited by 34
Yan, J., den Camp, H. J. M. O., Jetten, M. S. M., Hu, Y. Y., & Haaijer, S. C. M. (2010) · Systematic and Applied Microbiology · doi:10.1016/j.syapm.2010.08.003 · Cited by 34
Echalier, A., Brittain, T., Wright, J., Boycheva, S., Mortuza, G. B., Fülöp, V., & Watmough, N. J. (2008) · Biochemistry · doi:10.1021/bi702064f · Cited by 34
Silvestrini, M. C., Cutruzzolà, F., D'Alessandro, R., Brunori, M., Fochesato, N., & Zennaro, E. (1992) · Biochemical Journal · doi:10.1042/bj2850661 · Cited by 34
The human brain hexacoordinated neuroglobin three-dimensional structure
Pesce, A., Dewilde, S., Nardini, M., Moens, L. J., Ascenzi, P., Hankeln, T., Burmester, T., & Bolognesi, M. (2003) · Micron · doi:10.1016/j.micron.2003.10.013 · Cited by 34
Gordon, E., Sjögren, T., Löfqvist, M., Richter, C. D., Allen, J. W. A., Higham, C. W., Hajdu, J., Fülöp, V., & Ferguson, S. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211886200 · Cited by 34
Possible Neuroprotective Mechanism of Human Neuroglobin
Wakasugi, K. (2005) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1344.020 · Cited by 34
Metmyoglobin‐Catalyzed Exogenous and Endogenous Tyrosine Nitration by Nitrite and Hydrogen Peroxide
Nicolis, S., Monzani, E., Roncone, R., Gianelli, L., & Casella, L. (2004) · Chemistry - A European Journal · doi:10.1002/chem.200304989 · Cited by 33
Domanov, Y. A., Molotkovsky, J. G., & Gorbenko, G. P. (2005) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2005.09.002 · Cited by 33
Iron porphyrin-based electrocatalytic reduction of nitrite to ammonia
Barley, M. H., Takeuchi, K. J., Murphy, W. R., & Mayer, T. J. (1985) · Journal of the Chemical Society Chemical Communications · doi:10.1039/c39850000507 · Cited by 33
Catalytic Reduction of Dioxygen and Nitrite Ion at a Met80Ala Cytochrome c-Functionalized Electrode
Casalini, S., Battistuzzi, G., Borsari, M., Ranieri, A., & Sola, M. (2008) · Journal of the American Chemical Society · doi:10.1021/ja8040724 · Cited by 33
van Dalen, C. J., Winterbourn, C. C., & Kettle, A. J. (2006) · Biochemical Journal · doi:10.1042/bj20051470 · Cited by 33
Nagababu, E., Ramasamy, S., & Rifkind, J. M. (2007) · Biochemistry · doi:10.1021/bi700364e · Cited by 33
Vickers, S., Schiller, H. J., Hildreth, J. E. K., & Bulkley, G. B. (1998) · Surgery · doi:10.1016/s0039-6060(98)70102-3 · Cited by 33
Kurnikov, I. V., Ratner, M. A., & Pacheco, A. A. (2005) · Biochemistry · doi:10.1021/bi048060v · Cited by 33
Liposome effect on the cytochrome c-catalyzed peroxidation of carbonyl substrates to triplet species
Nantes, I. L., Faljoni‐Alário, A., Vercesi, A. E., Santos, K. E., & Bechara, E. J. H. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(98)00082-3 · Cited by 33
The enzymology of nitric oxide in bacterial pathogenesis and resistance
Crane, B. R. (2008) · Biochemical Society Transactions · doi:10.1042/bst0361149 · Cited by 33
Sundararajan, M., Hillier, I. H., & Burton, N. A. (2007) · The Journal of Physical Chemistry B · doi:10.1021/jp066852o · Cited by 32
Rudolf, M., Einsle, O., Neese, F., & Kroneck, P. M. H. (2002) · Biochemical Society Transactions · doi:10.1042/bst0300649 · Cited by 32
Probing the Role of the Internal Disulfide Bond in Regulating Conformational Dynamics in Neuroglobin
Astudillo, L., Bernad, S., Derrien, V., Sebban, P., & Mikšovská, J. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2010.04.033 · Cited by 32
Quantitative measurements of NO reaction kinetics with a Clark-type electrode
Liu, X., Liu, Q., Gupta, E., Zorko, N. A., Brownlee, E., & Zweier, J. L. (2005) · Nitric Oxide · doi:10.1016/j.niox.2005.04.011 · Cited by 32
Huang, K. T., Azarov, I., Basu, S., Huang, J., & Kim‐Shapiro, D. B. (2005) · Blood · doi:10.1182/blood-2005-10-4104 · Cited by 32
Immuno-spin trapping of hemoglobin and myoglobin radicals derived from nitrite-mediated oxidation
Keszler, Á., Mason, R. P., & Hogg, N. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.09.005 · Cited by 32
Mahro, M., Coelho, C., Trincão, J., Rodrigues, D., Terao, M., Garattini, E., Saggu, M., Lendzian, F., Hildebrandt, P., Romão, M. J., et al. (2011) · Drug Metabolism and Disposition · doi:10.1124/dmd.111.040873 · Cited by 32
Day, E. P., Peterson, J., Bonvoisin, J., Young, L. J., Wilkerson, J. O., & Siegel, L. M. (1988) · Biochemistry · doi:10.1021/bi00406a046 · Cited by 32
Deligeer, Fukunaga, R., Kataoka, K., Yamaguchi, K., Kobayashi, K., Tagawa, S., & Suzuki, S. (2002) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(02)00442-7 · Cited by 32
Multiple haem lyase genes indicate substrate specificity in cytochrome c biogenesis
Hartshorne, S., Richardson, D. J., & Simon, J. (2006) · Biochemical Society Transactions · doi:10.1042/bst0340146 · Cited by 32
Wu, M., van Alen, T. A., van Donselaar, E. G., Strous, M., Jetten, M. S. M., & van Niftrik, L. A. (2012) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2012.02615.x · Cited by 32
Nayak, G., Prentice, H. M., & Milton, S. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06157.x · Cited by 31
Superoxide Production during Reduction of Molecular Oxygen by Assimilatory Nitrate Reductase
Barber, M. J., & Kay, C. (1996) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1996.0069 · Cited by 31
Rodrigues, M. L., Oliveira, T. F., Matias, P. M., Martins, I. C., Valente, F. M. A., Pereira, I. A. C., & Archer, M. (2006) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309106016629 · Cited by 31
Okamoto, K., & Nishino, T. (2008) · Journal of Nippon Medical School · doi:10.1272/jnms.75.2 · Cited by 31
Azoreductase activity by purified rabbit liver aldehyde oxidase
Stoddart, A. M., & Levine, W. G. (1992) · Biochemical Pharmacology · doi:10.1016/0006-2952(92)90182-i · Cited by 31
Cantú‐Medellín, N., Vitturi, D. A., Rodriguez, C. A., Murphy, S. M., Dorman, S. C., Shiva, S., Zhou, Y., Jia, Y., Palmer, A. F., & Patel, R. P. (2011) · Nitric Oxide · doi:10.1016/j.niox.2011.01.006 · Cited by 31
XXIV. Researches on the blood.—On the action of nitrites on blood
Gamgee, A. (1868) · Philosophical Transactions of the Royal Society of London · doi:10.1098/rstl.1868.0025 · Cited by 31
Kuznetsova, S. A., Knaff, D. B., Hirasawa, M., Setif, P. Q. Y., & Mattioli, T. A. (2004) · Biochemistry · doi:10.1021/bi048826r · Cited by 31
Redox Properties of Cytochrome Nitrite Reductase from ATCC 27774
Costa, C., Moura, J. J. G., Moura, I., Wang, Y., & Huynh, B. H. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.38.23191 · Cited by 31
Self-citationDoes the Reduction of c Heme Trigger the Conformational Change of Crystalline Nitrite Reductase?
Nurizzo, D., Cutruzzolà, F., Arese, M., Bourgeois, D., Brunori, M., Cambillau, C., & Tegoni, M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.21.14997 · Cited by 31
Rajapakshe, A., Snyder, R. A., Astashkin, A. V., Bernardson, P., Evans, D. J., Young, C. G., Evans, D. H., & Enemark, J. H. (2009) · Inorganica Chimica Acta · doi:10.1016/j.ica.2009.05.040 · Cited by 31
van Wonderen, J. H., Kostrz, D. N., Dennison, C., & MacMillan, F. (2013) · Angewandte Chemie International Edition · doi:10.1002/anie.201208166 · Cited by 31
Chen, C.-S., & Yeh, W. (2010) · Chemical Communications · doi:10.1039/b927513d · Cited by 31
≥95% of xanthine oxidase in human milk is present as the demolybdo form, lacking molybdopterin
GODBER, B. L. J., Sanders, S. A., Harrison, R., Eisenthal, R., & Bray, R. C. (1997) · Biochemical Society Transactions · doi:10.1042/bst025519s · Cited by 31
Rinaldo, S., Sam, K. A., Castiglione, N., Stelitano, V., Arcovito, A., Brunori, M., Allen, J. W. A., Ferguson, S. J., & Cutruzzolà, F. (2011) · Biochemical Journal · doi:10.1042/bj20101615 · Cited by 30
Lü, D., Dong, J., Jin, H., Sun, L., Xu, X., Zhou, T., Zhu, Y., & Xu, M. (2011) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-011-3146-1 · Cited by 30
Peroxynitrite formation from the simultaneous reduction of nitrite and oxygen by xanthine oxidase
Millar, T. M. (2004) · FEBS Letters · doi:10.1016/s0014-5793(04)00218-2 · Cited by 30
Identification of superoxide production by Arabidopsis thaliana aldehyde oxidases AAO1 and AAO3
Zarepour, M., Simon, K., Wilch, M., Nieländer, U., Koshiba, T., Seo, M., Lindel, T., & Bittner, F. (2012) · Plant Molecular Biology · doi:10.1007/s11103-012-9975-1 · Cited by 30
Denitrification by the FungusFusarium oxysporumInvolves NADH-Nitrate Reductase
Fujii, T., & Takaya, N. (2008) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.70538 · Cited by 30
Measurement of physiological S-nitrosothiols: a problem child and a challenge
Tsikas, D. (2003) · Nitric Oxide · doi:10.1016/s1089-8603(03)00044-2 · Cited by 30
Tocheva, E. I., Eltis, L. D., & Murphy, M. E. P. (2008) · Biochemistry · doi:10.1021/bi7020537 · Cited by 30
Dixon, M., & Thurlow, S. (1924) · Biochemical Journal · doi:10.1042/bj0180989 · Cited by 30
Leferink, N. G. H., Eady, R. R., Hasnain, S. S., & Scrutton, N. S. (2012) · FEBS Journal · doi:10.1111/j.1742-4658.2012.08601.x · Cited by 29
The crystal structure of K3Cu(NO2)3
KLANDERMAN, K. A., Hamilton, W. C., & Bernal, I. (1977) · Inorganica Chimica Acta · doi:10.1016/s0020-1693(00)94751-0 · Cited by 29
Formation of nitrite from nitrate at the dorsum linguae.
Sasaki, T., & MATANO, K. (1979) · Food Hygiene and Safety Science (Shokuhin Eiseigaku Zasshi) · doi:10.3358/shokueishi.20.363 · Cited by 29
de Marothy, S. A., Blomberg, M. R. A., & Siegbahn, P. E. M. (2006) · Journal of Computational Chemistry · doi:10.1002/jcc.20567 · Cited by 29
Hough, M. A., Eady, R. R., & Hasnain, S. S. (2008) · Biochemistry · doi:10.1021/bi801369y · Cited by 29
Maia, L. B., Vala, A., & Mira, L. (2005) · Free Radical Research · doi:10.1080/10715760500210962 · Cited by 29
Self-citationSetif, P. Q. Y., Hirasawa, M., Cassan, N., Lagoutte, B., Tripathy, J. N., & Knaff, D. B. (2009) · Biochemistry · doi:10.1021/bi802096f · Cited by 29
The Structure of an Alternative Form ofParacoccus pantotrophus Cytochromecd 1 Nitrite Reductase
Sjögren, T., & Hajdu, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103657200 · Cited by 29
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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