How Biology Handles Nitrite

Crystal structure of the carbon monoxide complex of human cytoglobin

Makino, M., Sawai, H., Shiro, Y., & Sugimoto, H. (2010) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22950 · Cited by 29

Intramolecular Electron Transfer in Pseudomonas aeruginosa cd1 Nitrite Reductase: Thermodynamics and Kinetics

Farver, O., Brunori, M., Cutruzzolà, F., Rinaldo, S., Wherland, S. E., & Pecht, I. (2009) · Biophysical Journal · doi:10.1016/j.bpj.2008.12.3937 · Cited by 29

Ferricytochrome c protects mitochondrial cytochrome c oxidase against hydrogen peroxide-induced oxidative damage

Sedlák, E., Fabián, M., Robinson, N. C., & Musatov, A. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.08.019 · Cited by 29

The nitrite oxidizing system ofNitrobacter winogradskyi

Yamanaka, T., & Fukumori, Y. (1988) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1988.tb02746.x · Cited by 29

Reductive nitrosylation of ferric human serum heme‐albumin

Ascenzi, P., Cao, Y., di Masi, A., Gullotta, F., Sanctis, G. D., Fanali, G., Fasano, M., & Coletta, M. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07662.x · Cited by 28

The Heparin-Binding Site of Human Xanthine Oxidase.

FUKUSHIMA, T., Adachi, T., & Hirano, K. (1995) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.18.156 · Cited by 28

Catalysis of intermolecular oxygen atom transfer by nitrite dehydrogenase of Nitrobacter agilis.

Friedman, S., Massefski, W. W., & Hollocher, T. C. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)67418-6 · Cited by 28

Soluble and Plasma Membrane-bound Enzymes Involved in Nitrate and Nitrite Metabolism

Meyer, C., & Stöhr, C. (2002) · Advances in photosynthesis and respiration · doi:10.1007/0-306-48138-3_4 · Cited by 28

Comparative structural and functional analysis of two octaheme nitrite reductases from closely related T hioalkalivibrio species

Tikhonova, T. V., Tikhonov, A. V., Trofimov, A. A., Polyakov, K. M., Boyko, K. M., Cherkashin, E., Rakitina, T. V., Sorokin, D. Y., & Popov, V. O. (2012) · FEBS Journal · doi:10.1111/j.1742-4658.2012.08811.x · Cited by 28

Reactivity of glass-embedded met hemoglobin derivatives toward external NO: implications for nitrite-mediated production of bioactive NO

Navati, M. S., & Friedman, J. M. (2009) · Journal of the American Chemical Society · doi:10.1021/ja903364h · Cited by 28

Purification of Xanthine Oxidase from human heart

Abadeh, S., Case, P., & Harrison, R. (1993) · Biochemical Society Transactions · doi:10.1042/bst021099s · Cited by 28

Analysis of the Magnetic Properties of Nitrogenase FeMo Cofactor by Single‐Crystal EPR Spectroscopy

Spatzal, T., Einsle, O., & Andrade, S. L. A. (2013) · Angewandte Chemie International Edition · doi:10.1002/anie.201303000 · Cited by 28

Nitrite transport into pig erythrocytes and its potential biological role

Jensen, F. B. (2005) · Acta Physiologica Scandinavica · doi:10.1111/j.1365-201x.2005.01448.x · Cited by 28

Enzymatic activity mastered by altering metal coordination spheres

Moura, I., Pauleta, S. R., & Moura, J. J. G. (2008) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-008-0414-3 · Cited by 28

Spinach Ferredoxin-Nitrite Reductase: Characterization of Catalytic Activity and Interaction of the Enzyme with Substrates

Mikami, B., & Ida, S. (1989) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a122617 · Cited by 27

Immunochemical detection of nitric oxide and nitrogen dioxide trapping of the tyrosyl radical and the resulting nitrotyrosine in sperm whale myoglobin

Nakai, K., & Mason, R. P. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.05.019 · Cited by 27

Molecular oxygen as electron acceptor in the NADH-nitrate reductase system

Ruoff, P., & Lillo, C. (1990) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(90)91545-4 · Cited by 27

Mechanistic Studies on the Nitrite-Catalyzed Reductive Nitrosylation of Highly Charged Anionic and Cationic FeIIIPorphyrin Complexes

Jee, J., & van Eldik, R. (2006) · Inorganic Chemistry · doi:10.1021/ic0603104 · Cited by 27

Emerging role of nitrite in myocardial protection

Lefer, D. J. (2009) · Archives of Pharmacal Research · doi:10.1007/s12272-009-1804-y · Cited by 27

ARTICLE XI. ON THE PHYSIOLOGICAL ACTION OF POTASSIUM NITRITE

REICHERT, E. T., & MITCHELL, S. W. (1880) · The American Journal of the Medical Sciences · doi:10.1097/00000441-188007000-00011 · Cited by 27

Molybdenum Induces the Expression of a Protein Containing a New Heterometallic Mo-Fe Cluster in Desulfovibrio alaskensis

Rivas, M. G., Carepo, M. S. P., Mota, C., Korbas, M., Durand, M.-C., Lopes, A. T., Brondino, C. D., Pereira, A. S., George, G. N., Dolla, A. R., et al. (2009) · Biochemistry · doi:10.1021/bi801773t · Cited by 27

Hydroxylation of 4-amino-antifolates by partially purified aldehyde oxidase from rabbit liver

Fabre, G., Seither, R. L., & Goldman, I. D. (1986) · Biochemical Pharmacology · doi:10.1016/0006-2952(86)90277-7 · Cited by 27

Kinetic studies on the oxidation of nitrite by horseradish peroxidase and lactoperoxidase.

Gȩbicka, L. (1999) · Acta Biochimica Polonica · doi:10.18388/abp.1999_4114 · Cited by 27

Insights into Redox Partner Interactions and Substrate Binding in Nitrite Reductase from Alcaligenes xylosoxidans: Crystal Structures of the Trp138His and His313Gln Mutants,

Barrett, M. L., Harris, R. L., Antonyuk, S. V., Hough, M. A., Ellis, M. J., Sawers, R. G., Eady, R. R., & Hasnain, S. S. (2004) · Biochemistry · doi:10.1021/bi048682g · Cited by 27

Cytochrome c nitrite reductase: from structural to physicochemical analysis

Burlat, B., Gwyer, J. D., Poock, S. R., Clarke, T. A., Cole, J. A., Hemmings, A. M., Cheesman, M. R., Butt, J. N., & Richardson, D. J. (2005) · Biochemical Society Transactions · doi:10.1042/bst0330137 · Cited by 27

Catalytic and spectroscopic analysis of blue copper-containing nitrite reductase mutants altered in the environment of the type 2 copper centre: implications for substrate interaction

Prudêncio, M., Eady, R. R., & Sawers, R. G. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3530259 · Cited by 27

Redox Properties of Lysine- and Methionine-Coordinated Hemes Ensure Downhill Electron Transfer in NrfH2A4 Nitrite Reductase

Todorović, S., Rodrigues, M. L., Matos, D., & Pereira, I. A. C. (2012) · The Journal of Physical Chemistry B · doi:10.1021/jp301356m · Cited by 27

63 The Role of Heme-Nitrosyls in the Biosynthesis, Transport, Sensing, and Detoxification of Nitric Oxide in Biological Systems: Enzymes and Model Complexes

Lehnert, N., Berto, T. C., Galinato, M. G. I., & Goodrich, L. E. (2011) · Handbook of porphyrin science · doi:10.1142/9789814322386_0015 · Cited by 27

Effects of nitric oxide donors on cardiac contractility in wild‐type and myoglobin‐deficient mice

Wegener, J. W., Gödecke, A., Schrader, J., & Nawrath, H. (2002) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0704740 · Cited by 26

PHOTOOXIDATIVE AND SPECTRAL STUDIES ON CYTOCHROME c. CONFORMATIONAL CHANGES INDUCED BY BINDING OF CARDIOLIPIN

Jori, G., Tamburro, A. M., & Azzi, A. (1974) · Photochemistry and Photobiology · doi:10.1111/j.1751-1097.1974.tb06521.x · Cited by 26

Characterization of the Association of Nitrate Reductase with Barley (Hordeum vulgare L.) Root Membranes

Meyerhoff, P. A., Fox, T. C., Travis, R. L., & Huffaker, R. C. (1994) · PLANT PHYSIOLOGY · doi:10.1104/pp.104.3.925 · Cited by 25

Structure and evolution of Paramecium hemoglobin genes

Yamauchi, K., Tada, H., & Usuki, I. (1995) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/0167-4781(95)00114-v · Cited by 25

Comparison of the structural and kinetic properties of the cytochrome c nitrite reductases from Escherichia coli, Wolinella succinogenes, Sulfurospirillum deleyianum and Desulfovibrio desulfuricans

Clarke, T. A., Hemmings, A. M., Burlat, B., Butt, J. N., Cole, J. A., & Richardson, D. J. (2006) · Biochemical Society Transactions · doi:10.1042/bst0340143 · Cited by 25

Decomposition of hydroxylamine by hemoglobin

Bazylinski, D. A., Arkowitz, R. A., & Hollocher, T. C. (1987) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(87)90518-2 · Cited by 25

Nitrate reductase-dependent nitric oxide synthesis in the defense response of Arabidopsis thaliana against Pseudomonas syringae

Oliveira, H. C., Saviani, E. E., de Oliveira, J. A., & Salgado, I. (2010) · Tropical Plant Pathology · doi:10.1590/s1982-56762010000200005 · Cited by 25

Involvement of a single thiol group in the conversion of the NAD+-dependent activity of rat liver xanthine oxidoreductase to the O2-dependent activity

Kamiński, Z., & Jeżewska, M. (1982) · Biochemical Journal · doi:10.1042/bj2070341 · Cited by 25

Polycations Globally Enhance Binding of 14-3-3ω to Target Proteins in Spinach Leaves

Shen, W., & Huber, S. C. (2006) · Plant and Cell Physiology · doi:10.1093/pcp/pcj050 · Cited by 25

Oxidation of oxymyoglobin by nitric oxide through dissociation from cobalt nitrosyls

Doyle, M. P., Pickering, R. A., & Cook, B. R. (1983) · Journal of Inorganic Biochemistry · doi:10.1016/0162-0134(83)80006-3 · Cited by 25

The Interaction of Spinach Nitrite Reductase with Ferredoxin: A Site-Directed Mutation Study

Hirasawa, M., Tripathy, J. N., Ramasamy, S., Johnson, M. K., Bhalla, M., Allen, J. P., & Knaff, D. B. (2009) · Molecular Plant · doi:10.1093/mp/ssn098 · Cited by 25

Helicobacter pylori from duodenal ulcer patients expresses inducible nitric oxide synthase immunoreactivity in vivo and in vitro.

Stachura, J., Konturek, J. W., Karczewska, A., Domschke, W., Popiela, T. J., & Konturek, S. (1996) · PubMed · Cited by 24

Protection From Ischemic Cell Death by the Induction of Cytoglobin

Stagner, J. I., Parthasarathy, S. N., Wyler, K., & Parthasarathy, R. N. (2005) · Transplantation Proceedings · doi:10.1016/j.transproceed.2005.10.001 · Cited by 24

Investigation of the Mechanism of Action of Microperoxidase-11, (MP11), a Potential Anti-cataract Agent, with Hydrogen Peroxide and Ascorbate

Spector, A., Zhou, W., Ma, W., Chignell, C. F., & Reszka, K. J. (2000) · Experimental Eye Research · doi:10.1006/exer.2000.0867 · Cited by 24

An electron paramagnetic resonance study of the affinity of nitrite for methemoglobin

Goetz, B. I., Shields, H. W., Basu, S., Wang, P., King, S. B., Hogg, N., Gladwin, M. T., & Kim‐Shapiro, D. B. (2009) · Nitric Oxide · doi:10.1016/j.niox.2009.10.009 · Cited by 24

The Proportion of Xanthine Oxidase Activity of Total Xanthine Oxidoreductase Activity In Situ Remains Constant in Rat Liver Under Various (Patho)Physiological Conditions

Frederiks, W. M., & Bosch, K. S. (1996) · Hepatology · doi:10.1002/hep.510240533 · Cited by 24

A Eukaryotic Copper-Containing Nitrite Reductase Derived from a NirK Homolog Gene ofAspergillus oryzae

Nakanishi, Y., Zhou, S., Sang-Wan, K. I. M., Fushinobu, S., Maruyama, J., Kitamoto, K., Wakagi, T., & Shoun, H. (2010) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.90844 · Cited by 24

Heterodimeric nitrate reductase (NapAB) fromCupriavidus necatorH16: purification, crystallization and preliminary X-ray analysis

Coelho, C., González, P. J., Trincão, J., Carvalho, A. L., Najmudin, S., Hettman, T., Dieckman, S., Moura, J. J. G., Moura, I., & Romão, M. J. (2007) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309107022129 · Cited by 24

Characterization of ammonia-ligated low-spin iron(III) porphyrin complexes

Kim, Y. O., & Goff, H. M. (1990) · Inorganic Chemistry · doi:10.1021/ic00344a054 · Cited by 24

A reassessment of the genetic determinants, the effect of growth conditions and the availability of an electron donor on the nitrosating activity of Escherichia coli K-12

Metheringham, R. L., & Cole, J. A. (1997) · Microbiology · doi:10.1099/00221287-143-8-2647 · Cited by 24

Prosthetic group content and ligand-binding properties of spinach nitrite reductase.

Hirasawa, M., Shaw, R. W., Palmer, G., & Knaff, D. B. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45221-0 · Cited by 23

Production of nitrous oxide from nitrite in Klebsiella pneumoniae: mutants altered in nitrogen metabolism

Satoh, T., Hom, S. S. M., & Shanmugam, K. T. (1983) · Journal of Bacteriology · doi:10.1128/jb.155.2.454-458.1983 · Cited by 23

The changes of nitric oxide production during the growth of Microcystis aerugrinosa

Tang, X., Chen, J., Wang, W., Liu, T., Zhang, J., Gao, Y., Pei, Z., & Zheng, H. (2011) · Environmental Pollution · doi:10.1016/j.envpol.2011.06.042 · Cited by 23

Effects of long term nitrite therapy on functional recovery in experimental ischemia model

Jung, K.-H., Chu, K., Lee, S.-T., Sunwoo, J.-S., Park, D.-K., Kim, J.-H., Kim, S., Lee, S. K., Kim, M., & Roh, J.-K. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.10.116 · Cited by 23

Allosteric effects on oxidative and nitrosative reactions of cell‐free hemoglobins

Bonaventura, C., Henkens, R. W., Alayash, A. I., & Crumbliss, A. L. (2007) · IUBMB Life · doi:10.1080/15216540601188546 · Cited by 23

Expression and characterization of the assimilatory NADH-nitrite reductase from the phototrophic bacterium Rhodobacter capsulatus E1F1

Olmo-Mira, M. F., Cabello, P., Pino, C., Martínez‐Luque, M., Richardson, D. J., del Castillo, F. J., Roldán, M. D., & Moreno‐Vivián, C. (2006) · Archives of Microbiology · doi:10.1007/s00203-006-0149-x · Cited by 23

Structural and mechanistic insights into the electron flow through protein for cytochrome c-tethering copper nitrite reductase

Tsuda, A., Ishikawa, R., Koteishi, H., Tange, K., Fukuda, Y., Kobayashi, K., Tsuyoshi Inoue, A., & Nojiri, M. (2013) · The Journal of Biochemistry · doi:10.1093/jb/mvt023 · Cited by 23

Binding of NO and CO to the d1 Heme of cd1 Nitrite Reductase from Pseudomonas aeruginosa

Das, T. K., Wilson, E. K., Cutruzzolà, F., Brunori, M., & Rousseau, D. L. (2001) · Biochemistry · doi:10.1021/bi002327i · Cited by 23

Evidence of a two-fold mechanism responsible for the inhibition by allopurinol of the hypersensitive response induced in tobacco by tobacco necrosis virus

Montalbini, P., & Torre, G. D. (1996) · Physiological and Molecular Plant Pathology · doi:10.1006/pmpp.1996.0023 · Cited by 22

Mitochondria, Oxygen and Reperfusion Damage

Darley-Usmar, V. M., Stone, D. A., Smith, D. R., & Martin, J. F. (1991) · Annals of Medicine · doi:10.3109/07853899109150521 · Cited by 22

Identification of an intermolecular disulfide bond in barley hemoglobin

Bykova, N. V., Igamberdiev, A. U., Ens, W., & Hill, R. D. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.06.091 · Cited by 22

Characterization of the siroheme active site in spinach nitrite reductase by resonance Raman spectroscopy

Ondrias, M. R., Carson, S. D., Hirasawa, M., & Knaff, D. B. (1985) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(85)90023-8 · Cited by 22

Fluorescence Lifetime Analysis of Nitrite Reductase from Alcaligenes xylosoxidans at the Single‐Molecule Level Reveals the Enzyme Mechanism

Tabares, L. C., Kostrz, D. N., Elmalk, A. T., Andreoni, A., Dennison, C., Aartsma, T. J., & Canters, G. W. (2011) · Chemistry - A European Journal · doi:10.1002/chem.201102063 · Cited by 22

Nitrite Accumulation Within Herbicide-Treated Leaves

Klepper, L. A. (1976) · Weed Science · doi:10.1017/s0043174500062883 · Cited by 22

XANTHINE OXIDASE

Fridovich, I., & Handler, P. (1957) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)70690-x · Cited by 21

The Possible Involvement of Copper-Containing Nitrite Reductase (NirK) and Flavohemoglobin in Denitrification by the FungusCylindrocarpon tonkinense

Sang-Wan, K. I. M., Fushinobu, S., Zhou, S., Wakagi, T., & Shoun, H. (2010) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.100071 · Cited by 21

Sodium Nitrite Mitigates Ventilator-induced Lung Injury in Rats

Pickerodt, P. A., Emery, M. J., Zarndt, R., Martin, W., Francis, R. C. E., Boemke, W., & Swenson, E. R. (2012) · Anesthesiology · doi:10.1097/aln.0b013e3182655f80 · Cited by 21

Overexpression, purification, and biochemical and spectroscopic characterization of copper-containing nitrite reductase from Sinorhizobium meliloti 2011. Study of the interaction of the catalytic copper center with nitrite and NO

Ferroni, F. M., Guerrero, S. A., Rizzi, A. C., & Brondino, C. D. (2012) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2012.04.016 · Cited by 21

Cyanide Binding to cd1 Nitrite Reductase from Pseudomonas aeruginosa: Role of the Active-Site His369 in Ligand Stabilization

Sun, W., Arese, M., Brunori, M., Nurizzo, D., Brown, K., Cambillau, C., Tegoni, M., & Cutruzzolà, F. (2002) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2002.6391 · Cited by 21

Nitrite controls the release of nitric oxide in Pseudomonas aeruginosa cd1 nitrite reductase

Rinaldo, S., Brunori, M., & Cutruzzolà, F. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.09.036 · Cited by 21

DOMAIN SWING UPON HIS TO ALA MUTATION IN NITRITE REDUCTASE OF PSEUDOMONAS AERUGINOSA

Brown, K., Roig-Zamboni, V., Cutruzzolà, F., Arese, M., Sun, W., Brunori, M., Cambillau, C., & Tegoni, M. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4986 · Cited by 21

Nitrate Reductase- and Nitric Oxide-Dependent Activation of Sinapoylglucose:malate sinapoyltransferase in Leaves of Arabidopsis thaliana

Filho, P. R. D. S., Vitor, S. C., Frungillo, L., Saviani, E. E., Oliveira, H. C., & Salgado, I. (2012) · Plant and Cell Physiology · doi:10.1093/pcp/pcs104 · Cited by 21

Nitric oxide formation from the reaction of nitrite with carp and rabbit hemoglobin at intermediate oxygen saturations

Jensen, F. B. (2008) · FEBS Journal · doi:10.1111/j.1742-4658.2008.06486.x · Cited by 20

A New Paramagnetic Intermediate Formed during the Reaction of Nitrite with Deoxyhemoglobin

Salgado, M. T., Ramasamy, S., Tsuneshige, A., Manoharan, P. T., & Rifkind, J. M. (2011) · Journal of the American Chemical Society · doi:10.1021/ja1115088 · Cited by 20

New Insights into the Biological and Synthetic Fixation of Nitrogen

Scheibel, M. G., & Schneider, S. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201200175 · Cited by 20

Nonsymbiotic haemoglobins in plants.

Sowa, A., Guy, P. A., Sowa, S., & Hill, R. D. (1999) · Acta Biochimica Polonica · doi:10.18388/abp.1999_4175 · Cited by 20

Reductive nitrosylation of ferric cyanide horse heart myoglobin is limited by cyanide dissociation

Ascenzi, P., di Masi, A., Gullotta, F., Mattu, M., Ciaccio, C., & Coletta, M. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.01.092 · Cited by 20

Nitrite–methemoglobin inadequate for hypoxic vasodilation

Schwab, D. E., Stamler, J. S., & Singel, D. J. (2009) · Nature Chemical Biology · doi:10.1038/nchembio0609-366 · Cited by 19

NO reactions with sol-gel and solution phase samples of the ferric nitrite derivative of HbA

Roche, C. J., & Friedman, J. M. (2010) · Nitric Oxide · doi:10.1016/j.niox.2009.11.003 · Cited by 19

Circulating nitrite anions are a directly acting vasodilator and are donors for nitric oxide

Demoncheaux, E. A. G., Higenbottam, T., 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/cs20010232 · Cited by 19

Primary structure of Tetrahymena hemoglobins

Takagi, T., Iwaasa, H., Yuasa, H. J., Shikama, K., Takemasa, T., & Watanabe, Y. (1993) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/0167-4781(93)90245-9 · Cited by 19

Intramolecular Electron Transfer from c Heme to d1 Heme in Bacterial Cytochrome cd1 Nitrite Reductase Occurs over the Same Distances at Very Different Rates Depending on the Source of the Enzyme

Kobayashi, K., Koppenhöfer, A., Ferguson, S. J., Watmough, N. J., & Tagawa, S. (2001) · Biochemistry · doi:10.1021/bi002534i · Cited by 19

Inhibitors of the Molybdenum Cofactor Containing 4-Hydroxybenzoyl-CoA Reductase

Johannes, J., Unciuleac, M.-C., Friedrich, T., Warkentin, E., Ermler, U., & Boll, M. (2008) · Biochemistry · doi:10.1021/bi800137v · Cited by 18

Identification of an N‐hydroxyguanidine reducing activity of xanthine oxidase

Dambrova, M., Uhlén, S., Welch, C. J., & Wikberg, J. E. S. (1998) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1998.2570178.x · Cited by 18

Acidified nitrite as a potential antifungal agent

Anyim, M., Benjamin, N., & Wilks, M. (2005) · International Journal of Antimicrobial Agents · doi:10.1016/j.ijantimicag.2005.03.011 · Cited by 18

A novel variant of ferredoxin-dependent sulfite reductase having preferred substrate specificity for nitrite in the unicellular red alga Cyanidioschyzon merolae

Sekine, K., Sakakibara, Y., Hase, T., & Sato, N. (2009) · Biochemical Journal · doi:10.1042/bj20090581 · Cited by 18

Effect of ascorbic acid supplementation on nitric oxide metabolites and systolic blood pressure in rats exposed to lead

Amani, M., Noroozzadeh, A., Badalzadeh, R., & Ali, K. (2010) · Indian Journal of Pharmacology · doi:10.4103/0253-7613.64501 · Cited by 18

Pseudoazurin Dramatically Enhances the Reaction Profile of Nitrite Reduction by Paracoccus pantotrophus Cytochrome cd1 and Facilitates Release of Product Nitric Oxide

Sam, K. A., Fairhurst, S. A., THORNELEY, R. N. F., Allen, J. W. A., & Ferguson, S. J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800954200 · Cited by 18

Molybdenum in living systems

Hille, R., & Mendel, R. R. (2010) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2010.10.014 · Cited by 17

EPR investigation of the role of B10 phenylalanine in neuroglobin — Evidence that B10Phe mediates structural changes in the heme region upon disulfide-bridge formation

Ezhevskaya, M., Trandafir, F., Moens, L. J., Dewilde, S., & Doorslaer, S. V. (2011) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2011.05.020 · Cited by 17

Disproportionation of O‐Benzylhydroxylamine Catalyzed by a Ferric Bis‐Picket Fence Porphyrin Complex

McQuarters, A. B., Goodrich, L. E., Goodrich, C. M., & Lehnert, N. (2013) · Zeitschrift für anorganische und allgemeine Chemie · doi:10.1002/zaac.201300125 · Cited by 17

FAD-dependent enzymes involved in the metabolic oxidation of xenobiotics

Benedetti, M. S. (2010) · Annales Pharmaceutiques Françaises · doi:10.1016/j.pharma.2010.10.004 · Cited by 17

Structure–function relationship of assimilatory nitrite reductases from the leaf and root of tobacco based on high‐resolution structures

Nakano, S., Takahashi, M., Sakamoto, A., Morikawa, H., & Katayanagi, K. (2012) · Protein Science · doi:10.1002/pro.2025 · Cited by 17

The reductive reaction mechanism of tobacco nitrite reductase derived from a combination of crystal structures and ultraviolet–visible microspectroscopy

Nakano, S., Takahashi, M., Sakamoto, A., Morikawa, H., & Katayanagi, K. (2012) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.24094 · Cited by 17

Characterization of a novel copper-haem c dissimilatory nitrite reductase from Ralstonia pickettii

Han, C., Wright, G. S. A., Fisher, K., Rigby, S. E. J., Eady, R. R., & Hasnain, S. S. (2012) · Biochemical Journal · doi:10.1042/bj20111623 · Cited by 17

The human molybdenum hydroxylase gene family: co-conspirators in metabolic free-radical generation and disease

Wright, R. M., & Repine, J. E. (1997) · Biochemical Society Transactions · doi:10.1042/bst0250799 · Cited by 17

Novel spectroscopic aspects of type I copper in hyphomicrobium nitrite reductase

Suzuki, S., Kohzuma, T., Shidara, S., Ohki, K., & Aida, T. (1993) · Inorganica Chimica Acta · doi:10.1016/s0020-1693(00)82892-3 · Cited by 16

15N Chemically Induced Dynamic Nuclear Polarization during Reaction of N-Acetyl--tyrosine with the Nitrating Systems Nitrite/Hydrogen Peroxide/Horseradish Peroxidase and Nitrite/Hypochloric Acid

Lehnig, M. (2001) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2001.2494 · Cited by 16

Variants of the tetrahaem cytochrome c quinol dehydrogenase NrfH characterize the menaquinol-binding site, the haem c-binding motifs and the transmembrane segment

Kern, M., Einsle, O., & Simon, J. (2008) · Biochemical Journal · doi:10.1042/bj20080475 · Cited by 16

Bis(diimine)nitritocopper(II) cations: crystal and molecular structures of [Cu(phen)2(ONO)]BF4·H2O and [Cu(bipy)2(ONO)]HSO4{phen=1,10 phenanthroline, bipy=2,2′-bipyridine}

Hill, S. J., Hubberstey, P., & Li, W. (1997) · Polyhedron · doi:10.1016/s0277-5387(96)00571-2 · Cited by 16

Influence of Distal Residue B10 on CO Dynamics in Myoglobin and Neuroglobin

Nienhaus, K., & Nienhaus, G. U. (2007) · Journal of Biological Physics · doi:10.1007/s10867-008-9059-2 · Cited by 16

Catalytic and spectroscopic analysis of blue copper-containing nitrite reductase mutants altered in the environment of the type 2 copper centre: implications for substrate interaction

Prudêncio, M., Eady, R. R., & Sawers, R. G. (2001) · Biochemical Journal · doi:10.1042/bj3530259 · Cited by 16

Molybdenum in Nitrate Reductase and Nitrite Oxidoreductase

Kroneck, P. M. H., & Abt, D. J. (2002) · Metal ions in biological systems · doi:10.1201/9780203909331.ch10 · Cited by 16

Probing the Unusual Oxidation/Reduction Behavior ofParacoccus pantotrophusCytochromecd1Nitrite Reductase by Replacing a Switchable Methionine Heme Iron Ligand with Histidine

Zajicek, R. S., Cartron, M. L., & Ferguson, S. J. (2006) · Biochemistry · doi:10.1021/bi0604983 · Cited by 15

The crystal structure and EPR g-tensors of [Cuterpy(ONO)OH2]NO2·H2O

Allman, R., Kremer, S., & KUCHARZCYK, D. (1984) · Inorganica Chimica Acta · doi:10.1016/s0020-1693(00)81012-9 · Cited by 15

Nitrite and nitrate reduction by molybdenum centers of the nitrate reductase type: Computational predictions on the catalytic mechanism

Silaghi-Dumitrescu, R. L., Mich, M., Matyas, C., & Cooper, C. E. (2011) · Nitric Oxide · doi:10.1016/j.niox.2011.11.004 · Cited by 15

Characterization of two Cu-containing protein fragments obtained by limited proteolysis of Hyphomicrobiumdenitrificans A3151 nitrite reductase

Yamaguchi, K., Kobayashi, M., Kataoka, K., & Suzuki, S. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)02764-x · Cited by 14

Expression, and Molecular and Enzymatic Characterization of Cu-Containing Nitrite Reductase from a Marine Ammonia-Oxidizing Gammaproteobacterium, Nitrosococcus oceani

Kondo, K., Yoshimatsu, K., & Fujiwara, T. (2012) · Microbes and Environments · doi:10.1264/jsme2.me11310 · Cited by 14

Quantitation of hypoxanthine in plasma from patients with ischemic heart disease: adaption of a high-performance liquid chromatographic method

Himmel, H. M., Sadony, V., & Ravens, U. (1991) · Journal of Chromatography B Biomedical Sciences and Applications · doi:10.1016/0378-4347(91)80344-c · Cited by 14

Substrate Binding to a Nitrite Reductase Induces a Spin Transition

Martins, G. F., Rodrigues, L., Cunha, F., Matos, D., Hildebrandt, P., Murgida, D. H., Pereira, I. A. C., & Todorović, S. (2010) · The Journal of Physical Chemistry B · doi:10.1021/jp9118502 · Cited by 14

A Novel Conformer of Oxidized Paracoccus pantotrophus Cytochrome cd1 Observed by Freeze-Quench NIR-MCD Spectroscopy

Allen, J. W. A., Cheesman, M. R., Higham, C. W., Ferguson, S. J., & Watmough, N. J. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.4009 · Cited by 14

Very Early Reaction Intermediates Detected by Microsecond Time Scale Kinetics of Cytochrome cd1-catalyzed Reduction of Nitrite

Sam, K. A., Strampraad, M. J. F., de Vries, S., & Ferguson, S. J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804493200 · Cited by 14

Nitrate reductase from Triticum aestivum leaves: Regulation of activity and possible role in production of nitric oxide

Galeeva, E. I., Trifonova, T. V., Ponomareva, A. A., Viktorova, L. V., & Minibayeva, F. V. (2012) · Biochemistry (Moscow) · doi:10.1134/s0006297912040128 · Cited by 14

Conversion of Ammonia to Dinitrogen in Wastewater by Nitrosomonas europaea

Shrestha, N. K., Hadano, S., Kamachi, T., & Okura, I. (2001) · Applied Biochemistry and Biotechnology · doi:10.1385/abab:90:3:221 · Cited by 14

The quaternary hemoglobin conformation regulates the formation of the nitrite-induced bioactive intermediate and the dissociation of nitric oxide from this intermediate

Rifkind, J. M., Nagababu, E., & Ramasamy, S. (2011) · Nitric Oxide · doi:10.1016/j.niox.2011.01.001 · Cited by 14

A Radical Route for Nitrogenase Carbide Insertion

Boal, A. K., & Rosenzweig, A. C. (2012) · Science · doi:10.1126/science.1229088 · Cited by 14

Differential expression of the nitrite reductase gene family in tobacco as revealed by quantitative competitive RT-PCR

Kato, C. (2004) · Journal of Experimental Botany · doi:10.1093/jxb/erh182 · Cited by 14

Nitrite reduction: a ubiquitous function from a pre-aerobic past

Cutruzzolà, F., Rinaldo, S., Castiglione, N., Giardina, G., Pecht, I., & Brunori, M. (2009) · BioEssays · doi:10.1002/bies.200800235 · Cited by 13

Diurnal changes in nitrogen assimilation of tobacco roots

Stöhr, C., & Mäck, G. (2001) · Journal of Experimental Botany · doi:10.1093/jxb/52.359.1283 · Cited by 13

Nitrogen-15 nuclear magnetic resonance investigation of nitrite reductase-substrate interaction

Timkovich, R., & Cork, M. S. (1982) · Biochemistry · doi:10.1021/bi00259a012 · Cited by 13

Modelling the Electron‐Transfer Complex Between Aldehyde Oxidoreductase and Flavodoxin

Krippahl, L., Palma, P. N., Moura, I., & Moura, J. J. G. (2006) · European Journal of Inorganic Chemistry · doi:10.1002/ejic.200600418 · Cited by 13

Density Functional Theory Modeling of the Proposed Nitrite Anhydrase Function of Hemoglobin in Hypoxia Sensing

Berto, T. C., & Lehnert, N. (2011) · Inorganic Chemistry · doi:10.1021/ic2003854 · Cited by 13

Allopurinol, an inhibitor of purine catabolism, enhances susceptibility of tobacco to Tobacco mosaic virus

Silvestri, S., Murphy, A. M., Buonaurio, R., & Carr, J. P. (2008) · Virus Research · doi:10.1016/j.virusres.2008.05.018 · Cited by 11

Reaction of nitrite with human fetal oxyhemoglobin: A model simulation study with implications for blood flow regulation in sickle cell disease (SCD)

Salhany, J. M. (2009) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2009.11.001 · Cited by 11

Molecular interactions between multihaem cytochromes: probing the protein–protein interactions between pentahaem cytochromes of a nitrite reductase complex

Lockwood, C. W. J., Butt, J. N., Clarke, T. A., & Richardson, D. J. (2011) · Biochemical Society Transactions · doi:10.1042/bst0390263 · Cited by 11

Spectroscopic and Electrochemical Properties of Cytochrome c551 from Alcaligenes xylosoxidans GIFU 1051

Deligeer, Kataoka, K., Yamaguchi, K., & Suzuki, S. (2000) · Bulletin of the Chemical Society of Japan · doi:10.1246/bcsj.73.1839 · Cited by 11

Artefacts induced on c-type haem proteins by electrode surfaces

de Sousa, P. M. P., Pauleta, S. R., Gonçalves, M. L. S. S., Pettigrew, G. W., Moura, I., Moura, J. J. G., & dos Santos, M. M. C. (2010) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-010-0717-z · Cited by 10

In vitro and ex vivo xanthine oxidoreductase activity in rat and guinea-pig hearts using hypoxanthine or xanthine as substrate

Janssen, M., Tavenier, M., Koster, J. F., & de Jong, J. W. (1993) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(93)90048-d · Cited by 10

Heme d1 Nitrosyl Complex of cd1 Nitrite Reductase Studied by High-Field-Pulse Electron Paramagnetic Resonance Spectroscopy

Radoul, M., Centola, F., Rinaldo, S., Cutruzzolà, F., Pecht, I., & Goldfarb, D. (2009) · Inorganic Chemistry · doi:10.1021/ic802355y · Cited by 10

Lack of conversion of xanthine dehydrogenase to xanthine oxidase during warm renal ischemia

Cighetti, G., Puppo, M. D., Paroni, R. C., & Kienle, M. G. (1990) · FEBS Letters · doi:10.1016/0014-5793(90)81334-k · Cited by 10

A comparison by means of antisera and lectins of surface structures ofNitrobacter winogradskyi andN. agilis

Kalthoff, H., Fehr, S., Sundermeyer, H., Renwrantz, L. R., & Bock, E. (1979) · Current Microbiology · doi:10.1007/bf02602880 · Cited by 10

Nitrite-induced improved blood circulation associated with an increase in a pool of RBC-NO with no bioactivity

Rifkind, J. M., Nagababu, E., Cao, Z., Barbiro-Michaely, E., & Mayevsky, A. (2009) · Advances in experimental medicine and biology · doi:10.1007/978-0-387-85998-9_5 · Cited by 10

Ultracytochemischer Nachweis von Enzymen durch Reduktion von Kaliumhexacyanoferrat (III)

Dikov, A., Alexandrov, I., Russinova, A. I., & Boyadjieva-Michailova, A. (1988) · Acta Histochemica · doi:10.1016/s0065-1281(88)80080-1 · Cited by 9

Mechanism of Transition from Xanthine Dehydrogenase to Xanthine Oxidase: Effect of Guanidine-HCL or Urea on the Activity

Tsujii, A., & Nishino, T. (2008) · Nucleosides Nucleotides & Nucleic Acids · doi:10.1080/15257770802146569 · Cited by 9

Crystallization and preliminary X-ray analysis of a membrane-bound nitrite reductase fromDesulfovibrio desulfuricansATCC 27774

Dias, J. M. L., Cunha, C. A., Teixeira, S. C. M., Almeida, G., Costa, C., Lampreia, J., Moura, J. J. G., Moura, I., & Romão, M. J. (2000) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444999016066 · Cited by 9

Isolation and oligomeric composition of cytochrome c nitrite reductase from the haloalkaliphilic bacterium Thioalkalivibrio nitratireducens

Tikhonova, T. V., Slutskaya, E. S., Filimonenkov, A. A., Boyko, K. M., Kleimenov, S. Y., Konarev, P. V., Polyakov, K. M., Svergun, D. I., Trofimov, A. A., Khomenkov, V. G., et al. (2008) · Biochemistry (Moscow) · doi:10.1134/s0006297908020077 · Cited by 9

Denitrification by plant roots? New aspects of plant plasma membrane-bound nitrate reductase

Eick, M., & Stöhr, C. (2011) · PROTOPLASMA · doi:10.1007/s00709-011-0355-5 · Cited by 9

NADH oxidation by hypoxanthine dehydrogenase of avian kidney

Landon, E. J., & Mj, M. (1967) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(67)90098-9 · Cited by 9

Reagents effecting nitrosation

Williams, D. L. H. (2004) · Elsevier eBooks · doi:10.1016/b978-044451721-0/50002-5 · Cited by 8

Production of nitric oxide by human salivary peroxidase and by bovine lactoperoxidase

Palmerini, C. A., Marmottini, F., & Arienti, G. (2012) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.21407 · Cited by 8

Is Nitrotyrosine Generated in Human Erythrocytes in Circulation?

Kikugawa, K., Nakauchi, K., Beppu, M., Hiramoto, K., Ando, K., & Hayakawa, M. (2000) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.23.379 · Cited by 8

X‐Ray Crystal Structure of a Mutant Assimilatory Nitrite Reductase That Shows Sulfite Reductase‐Like Activity

Nakano, S., Takahashi, M., Sakamoto, A., Morikawa, H., & Katayanagi, K. (2012) · Chemistry & Biodiversity · doi:10.1002/cbdv.201100442 · Cited by 8

Unexpected dependence on pH of NO release from Paracoccus pantotrophus cytochrome cd1

Sam, K. A., Tolland, J. D., Fairhurst, S. A., Higham, C. W., Lowe, D. J., THORNELEY, R. N. F., Allen, J. W. A., & Ferguson, S. J. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.04.149 · Cited by 8

Iron–Sulfur Centers: New Roles for Ancient Metal Sites

Grazina, R., Pauleta, S. R., Moura, J. J. G., & Moura, I. (2013) · Elsevier eBooks · doi:10.1016/b978-0-08-097774-4.00308-9 · Cited by 7

Nitrite and Heme Globins

Shiva, S., Frizzell, S. A., & Gladwin, M. T. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-373866-0.00019-8 · Cited by 7

Determination of xanthine oxidoreductase forms: influence of reaction conditions

Martí, R., Varela, E., Pascual, C., & Segura, R. (2001) · Clinica Chimica Acta · doi:10.1016/s0009-8981(00)00390-9 · Cited by 7

Biochemists alcohol problem: a case of addiction to the wrong concepts?

KACSER, H. (1983) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(83)90096-8 · Cited by 6

Reply to 'Nitrite–methemoglobin inadequate for hypoxic vasodilation'

Goetz, B. I., Wang, P., Shields, H. W., Basu, S., Grubina, R., Huang, J., Conradie, J., Huang, Z., Jeffers, A. B., Jiang, A., et al. (2009) · Nature Chemical Biology · doi:10.1038/nchembio0609-367 · Cited by 6

Electrochemical and Spectroscopic Study on the Interaction of Cytochrome c with Anionic Lipid Vesicles

Wei‐Guo, J., Chang‐Wei, L., Ji‐Lin, T., Wu, Z., Shao‐Jun, D., & Er‐Kang, W. (2003) · Chinese Journal of Chemistry · doi:10.1002/cjoc.20030210514 · Cited by 5

The measurement of neutrophil myeloperoxidase by flow cytochemistry is influenced by the pseudoperoxidase activity of hemoglobin [letter; comment]

Hewitt, J., & Dm, R. (1991) · Blood · doi:10.1182/blood.v78.7.1891a.1891a · Cited by 5

The measurement of neutrophil myeloperoxidase by flow cytochemistry is influenced by the pseudoperoxidase activity of hemoglobin [letter; comment]

Hewitt, J., & Dm, R. (1991) · Blood · doi:10.1182/blood.v78.7.1891a.bloodjournal7871891a · Cited by 4

The microbial nitrogen-cycling network

Kuypers, M. M. M., Marchant, H. K., & Kartal, B. (2018) · Nature Reviews Microbiology · doi:10.1038/nrmicro.2018.9 · Cited by 4,563

Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation

Tejero, J., Shiva, S., & Gladwin, M. T. (2019) · Physiological Reviews · doi:10.1152/physrev.00036.2017 · Cited by 541

Recent advances in nanostructured heterogeneous catalysts for N-cycle electrocatalysis

Liang, J., Liu, Q., Alshehri, A. A., & Sun, X. (2022) · Nano Research Energy · doi:10.26599/nre.2022.9120010 · Cited by 417

Reduction of Substrates by Nitrogenases

Seefeldt, L. C., Yang, Z., Lukoyanov, D. A., Harris, D. F., Dean, D. R., Raugei, S., & Hoffman, B. M. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00556 · Cited by 412

Electrocatalytic nitrate/nitrite reduction to ammonia synthesis using metal nanocatalysts and bio-inspired metalloenzymes

Wang, J., Feng, T., Chen, J., Ramalingam, V., Li, Z., Kabtamu, D. M., He, J., & Fang, X. (2021) · Nano Energy · doi:10.1016/j.nanoen.2021.106088 · Cited by 304

Peroxynitrite Reactions and Diffusion in Biology

Radí, R. (1998) · Chemical Research in Toxicology · doi:10.1021/tx980096z · Cited by 172

Biochemistry of nitric oxide and its redox-activated forms

Stamler, J. S., Singel, D. J., & Loscalzo, J. (1992) · Science · doi:10.1126/science.1281928 · Cited by 2,744

Reductive Transformations of Nitrite in Natural and Biomimetic Systems

Kundu, S., & Gupta, S. (2026) · Wiley eBooks · doi:10.1002/9781119951438.eibc2901

Dissimilatory Nitrite and Nitric Oxide Reductases

Averill, B. A. (1996) · Chemical Reviews · doi:10.1021/cr950056p · Cited by 545

On the biological reduction of nitrates to nitrites.

Stefanelli, I., & Picci, G. (1950)