Bacterial respiration: a flexible process for a changing environment 1999 Fleming Lecture (Delivered at the 144th meeting of the Society for General Microbiology, 8 September 1999)

Richardson, David J.

doi:10.1099/00221287-146-3-551

Cited by 544Bacterial Genetics and BiotechnologyMicrobial metabolism and enzyme functionRedox biology and oxidative stress

Bacterial respiration: a flexible process for a changing environment 1999 Fleming Lecture (Delivered at the 144th meeting of the Society for General Microbiology, 8 September 1999)

Richardson, David J.·2000·Microbiology

DOI 10.1099/00221287-146-3-551

Open this paper in CoChat — free account

Abstract

Microbiology Society journals contain high-quality research papers and topical review articles. We are a not-for-profit publisher and we support and invest in the microbiology community, to the benefit of everyone. This supports our principal goal to develop, expand and strengthen the networks available to our members so that they can generate new knowledge about microbes and ensure that it is shared with other communities.

Integrity signals

Registry

Crossref · 10.1099/00221287-146-3-551

Cites

139 of 139 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Switching from aerobic respiration to various forms of anaerobic respiration to deal with low oxygen levels has been implicated as an important virulence attribute in several prokaryotic pathogens.
“switching from aerobic respiration to various forms of anaerobic respiration to deal with low oxygen levels has been implicated as an important virulence attribute in several prokaryotic pathogens [18],[19]”
From A Sterol-Regulatory Element Binding Protein Is Required for Cell Polarity, Hypoxia Adaptation, Azole Drug Resistance, and Virulence in Aspergillus fumigatus (2008) · cites this paper as [19]

The complete genome sequence of Escherichia coli K-12.
Blattner, F., Plunkett, G., Bloch, C., Perna, N., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C., Mayhew, G., et al. (1997) · Science · doi:10.1126/science.277.5331.1453 · Cited by 7,996 · see citing works
Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
Cole, S. T., Brosch, R., Parkhill, J., Garnier, T., Churcher, C., Harris, D., Gordon, S. V., Eiglmeier, K., Gas, S., Barry, C. E., et al. (1998) · Nature · doi:10.1038/31159 · Cited by 7,847 · see citing works
Whole-Genome Random Sequencing and Assembly of Haemophilus influenzae Rd
Fleischmann, R. D., Adams, M. D., White, O. R., Clayton, R. A., Kirkness, E. F., Kerlavage, A. R., Bult, C. J., Tomb, J.-F., Dougherty, B. A., Merrick, J. M., et al. (1995) · Science · doi:10.1126/science.7542800 · Cited by 5,641 · see citing works
The complete genome sequence of the gastric pathogen Helicobacter pylori
Tomb, J.-F., White, O., Kerlavage, A. R., Clayton, R. A., Sutton, G. G., Fleischmann, R. D., Ketchum, K. A., Klenk, H. P., Gill, S., Dougherty, B. A., et al. (1997) · Nature · doi:10.1038/41483 · Cited by 3,529 · see citing works
Self-citation
Cell biology and molecular basis of denitrification
Zumft, W. G. (1997) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.61.4.533-616.1997 · Cited by 3,483 · see citing works
Complete Genome Sequence of the Methanogenic Archaeon, Methanococcus jannaschii
Bult, C. J., White, O. R., Olsen, G. J., Zhou, L., Fleischmann, R. D., Sutton, G. G., Blake, J. A., Fitzgerald, L. M., Clayton, R. A., Gocayne, J. D., et al. (1996) · Science · doi:10.1126/science.273.5278.1058 · Cited by 2,086 · see citing works
Search for Past Life on Mars: Possible Relic Biogenic Activity in Martian Meteorite ALH84001
McKay, D. S., Gibson, E. K., Thomas-Keprta, K. L., Vali, H., Romanek, C. S., Clemett, S. J., Chillier, X. D. F., Maechling, C. R., & Zare, R. N. (1996) · Science · doi:10.1126/science.273.5277.924 · Cited by 1,883 · see citing works
Dissimilatory Fe(III) and Mn(IV) reduction
Lovley, D. R. (1991) · Microbiological Reviews · doi:10.1128/mr.55.2.259-287.1991 · Cited by 1,718 · see citing works
The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus
Klenk, H., Clayton, R. A., Tomb, J.-F., White, O. R., Nelson, K. E., Ketchum, K. A., Dodson, R. J., Gwinn, M. L., Hickey, E. K., Peterson, J. D., et al. (1997) · Nature · doi:10.1038/37052 · Cited by 1,410 · see citing works
Self-citation
Biochemistry of methanogenesis: a tribute to Marjory Stephenson:1998 Marjory Stephenson Prize Lecture
Thauer, R. K. (1998) · Microbiology · doi:10.1099/00221287-144-9-2377 · Cited by 1,112 · see citing works
Dissimilatory Fe(III) and Mn(IV) reduction.
Lovley, D. R. (1991) · Microbiological Reviews · doi:10.1128/mmbr.55.2.259-287.1991 · Cited by 845 · see citing works
The deep, hot biosphere.
Gold, T. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.13.6045 · Cited by 655 · see citing works
Reduction of uranium by Desulfovibrio desulfuricans
Lovley, D. R., & Phillips, E. J. (1992) · Applied and Environmental Microbiology · doi:10.1128/aem.58.3.850-856.1992 · Cited by 625 · see citing works
Enzymes and associated electron transport systems that catalyse the respiratory reduction of nitrogen oxides and oxyanions
Berks, B. C., Ferguson, S. J., Moir, J. W. B., & Richardson, D. J. (1995) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(95)00092-5 · Cited by 596 · see citing works
Self-citation
Crystal Structure of Formate Dehydrogenase H: Catalysis Involving Mo, Molybdopterin, Selenocysteine, and an Fe 4 S 4 Cluster
Boyington, J. C., Gladyshev, V. N., Khangulov, S. V., Stadtman, T. C., & Sun, P. D. (1997) · Science · doi:10.1126/science.275.5304.1305 · Cited by 596 · see citing works
Microbiological evidence for Fe(III) reduction on early Earth
Vargas, M., Kashefi, K., Blunt-Harris, E. L., & Lovley, D. R. (1998) · Nature · doi:10.1038/25720 · Cited by 518 · see citing works
MOLYBDENUM-COFACTOR–CONTAINING ENZYMES: Structure and Mechanism
Kisker, C., Schindelin, H., & Rees, D. C. (1997) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.66.1.233 · Cited by 515 · see citing works
PCR Detection of Genes Encoding Nitrite Reductase in Denitrifying Bacteria
Hallin, S., & Lindgren, P. (1999) · Applied and Environmental Microbiology · doi:10.1128/aem.65.4.1652-1657.1999 · Cited by 458 · see citing works
Bioremediation of metal contamination
Lovley, D. R., & Coates, J. D. (1997) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(97)80005-5 · Cited by 452 · see citing works
Crystal Structure of DMSO Reductase: Redox-Linked Changes in Molybdopterin Coordination
Schindelin, H., Kisker, C., Hilton, J. C., Rajagopalan, K. V., & Rees, D. C. (1996) · Science · doi:10.1126/science.272.5268.1615 · Cited by 451 · see citing works
Microbial Fe(III) reduction in subsurface environments
Lovley, D. R. (1997) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.1997.tb00316.x · Cited by 417 · see citing works
Structure of cytochrome c nitrite reductase
Einsle, O., Messerschmidt, A., Stach, P., Bourenkov, G. P., Bartunik, H. D., Huber, R., & Kroneck, P. M. H. (1999) · Nature · doi:10.1038/22802 · Cited by 389 · see citing works
Phylogenetic analysis of dissimilatory Fe(III)-reducing bacteria
Lonergan, D. J., Jenter, H. L., Coates, J. D., Phillips, E. J., Schmidt, T. M., & Lovley, D. R. (1996) · Journal of Bacteriology · doi:10.1128/jb.178.8.2402-2408.1996 · Cited by 380 · see citing works
Stimulated anoxic biodegradation of aromatic hydrocarbons using Fe(III) ligands
Lovley, D. R., Woodward, J. C., & Chapelle, F. H. (1994) · Nature · doi:10.1038/370128a0 · Cited by 367 · see citing works
Reduction of uranium by cytochrome c3 of Desulfovibrio vulgaris
Lovley, D. R., Widman, P. K., Woodward, J. C., & Phillips, E. J. (1993) · Applied and Environmental Microbiology · doi:10.1128/aem.59.11.3572-3576.1993 · Cited by 350 · see citing works
Bioremediation of organic and metal contaminants with dissimilatory metal reduction
Lovley, D. R. (1995) · Journal of Industrial Microbiology & Biotechnology · doi:10.1007/bf01569889 · Cited by 323 · see citing works
The roles of the two proton input channels in cytochrome c oxidase from Rhodobacter sphaeroides probed by the effects of site-directed mutations on time-resolved electrogenic intraprotein proton transfer
Konstantinov, A. A., Siletsky, S. A., Mitchell, D. M., et al. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.17.9085 · Cited by 318 · see citing works
Cloning and sequence of cymA, a gene encoding a tetraheme cytochrome c required for reduction of iron(III), fumarate, and nitrate by Shewanella putrefaciens MR-1
Myers, C. R., & Myers, J. M. (1997) · Journal of Bacteriology · doi:10.1128/jb.179.4.1143-1152.1997 · Cited by 297 · see citing works
Genes for a microaerobically induced oxidase complex in Bradyrhizobium japonicum are essential for a nitrogen-fixing endosymbiosis.
Preisig, O., Anthamatten, D., & Hennecke, H. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.8.3309 · Cited by 294 · see citing works
Pyrobaculum aerophilum sp. nov., a novel nitrate-reducing hyperthermophilic archaeum
V�lkl, P., Huber, R., Drobner, E., Rachel, R., Burggraf, S., Trincone, A., & STETTER, K. O. (1993) · Applied and Environmental Microbiology · doi:10.1128/aem.59.9.2918-2926.1993 · Cited by 291 · see citing works
Crystal structure of the first dissimilatory nitrate reductase at 1.9 Å solved by MAD methods
Dias, J. M., Than, M. E., Humm, A., Huber, R., Bourenkov, G. P., Bartunik, H. D., Bursakov, S., Calvete, J., Caldeira, J., Carneiro, C., et al. (1999) · Structure · doi:10.1016/s0969-2126(99)80010-0 · Cited by 286 · see citing works
Shewanella putrefaciens mtrB Encodes an Outer Membrane Protein Required for Fe(III) and Mn(IV) Reduction
Beliaev, A. S., & Saffarini, D. A. (1998) · Journal of Bacteriology · doi:10.1128/jb.180.23.6292-6297.1998 · Cited by 277 · see citing works
Combined heterotrophic nitrification and aerobic denitrification in Thiosphaera pantotropha and other bacteria
Robertson, L. A., & Kuenen, J. G. (1990) · Antonie van Leeuwenhoek · doi:10.1007/bf00403948 · Cited by 270 · see citing works
Inorganic nitrogen metabolism in bacteria
Richardson, D. J., & Watmough, N. J. (1999) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(99)80034-9 · Cited by 264 · see citing works
Self-citation
The genetic basis of tetrathionate respiration in Salmonella typhimurium
Hensel, M., Hinsley, A. P., Nikolaus, T., Sawers, R. G., & Berks, B. C. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01345.x · Cited by 253 · see citing works
Cytochrome oxidase evolved by tinkering with denitrification enzymes
Saraste, M., & Castresana, J. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)80228-9 · Cited by 245 · see citing works
The cytochrome bd quinol oxidase in Escherichia coli has an extremely high oxygen affinity and two oxygen-binding haems: implications for regulation of activity in vivo by oxygen inhibition
D'mello, R., Hill, S., & Poole, R. K. (1996) · Microbiology · doi:10.1099/00221287-142-4-755 · Cited by 244 · see citing works
Periplasmic and membrane‐bound respiratory nitrate reductases in Thiosphaera pantotropha
Bell, L. C., Richardson, D. J., & Ferguson, S. J. (1990) · FEBS Letters · doi:10.1016/0014-5793(90)80889-q · Cited by 241 · see citing works
Self-citation
Purification and Characterization of the Selenate Reductase from Thauera selenatis
Schröder, I., Rech, S., Krafft, T., & Macy, J. M. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.38.23765 · Cited by 239 · see citing works
The 2.8 Å structure of hydroxylamine oxidoreductase from a nitrifying chemoautotrophic bacterium, Nitrosomonas europaea
Igarashi, N., Moriyama, H., Fujiwara, T., Fukumori, Y., & Tanaka, N. (1997) · Nature Structural Biology · doi:10.1038/nsb0497-276 · Cited by 238 · see citing works
Reactions of nitric oxide with cytochrome c oxidase
Brudvig, G. W., Stevens, T. H., & Chan, S. I. (1980) · Biochemistry · doi:10.1021/bi00564a020 · Cited by 237 · see citing works
Purification and characterization of the respiratory arsenate reductase of Chrysiogenes arsenatis
Krafft, T., & Macy, J. M. (1998) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1998.2550647.x · Cited by 230 · see citing works
Dual response regulators (NarL and NarP) interact with dual sensors (NarX and NarQ) to control nitrate- and nitrite-regulated gene expression in Escherichia coli K-12
Rabin, R. S., & Stewart, V. J. (1993) · Journal of Bacteriology · doi:10.1128/jb.175.11.3259-3268.1993 · Cited by 223 · see citing works
The heme-copper oxidase family consists of three distinct types of terminal oxidases and is related to nitric oxide reductase
John van der, O. O. S. T., Boer, A. P. N. D., de Gier, J. L., et al. (1994) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1994.tb07067.x · Cited by 214 · see citing works
Thauera selenatis gen. nov., sp. nov., a Member of the Beta Subclass of Proteobacteria with a Novel Type of Anaerobic Respiration
Macy, J. M., Rech, S. A., Auling, G., Dorsch, M., Stackebrandt, E. S., & Sly, L. I. (1993) · International Journal of Systematic Bacteriology · doi:10.1099/00207713-43-1-135 · Cited by 201 · see citing works
Evolution of energetic metabolism: the respiration-early hypothesis
Castresana, J., & Saraste, M. (1995) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)89098-2 · Cited by 196 · see citing works
Reduction of Technetium by Desulfovibrio desulfuricans : Biocatalyst Characterization and Use in a Flowthrough Bioreactor
Lloyd, J. R., Ridley, J., Khizniak, T., Lyalikova, N. N., & Macaskie, L. E. (1999) · Applied and Environmental Microbiology · doi:10.1128/aem.65.6.2691-2696.1999 · Cited by 187 · see citing works
Nitrogen cycle enzymology
Ferguson, S. J. (1998) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(98)80059-8 · Cited by 177 · see citing works
Structure and function of a periplasmic nitrate reductase in Alcaligenes eutrophus H16
Siddiqui, R. A., Warnecke‐Eberz, U., Hengsberger, A., Schneider, B., Kostka, S., & Friedrich, B. (1993) · Journal of Bacteriology · doi:10.1128/jb.175.18.5867-5876.1993 · Cited by 175 · see citing works
Crystal structure of oxidized trimethylamine N -oxide reductase from Shewanella massilia at 2.5 å resolution 1 1Edited by R. Huber
Czjzek, M., Santos, J. D., Pommier, J., Giordano, G., Méjean, V., & Haser, R. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2156 · Cited by 173 · see citing works
Respiratory Protection of Nitrogenase Activity in Azotobacter vinelandii—Roles of the Terminal Oxidases
Poole, R. K., & Hill, S. (1997) · Bioscience Reports · doi:10.1023/a:1027336712748 · Cited by 171 · see citing works
Anaerobic respiration in the Rhodospirillaceae: characterisation of pathways and evaluation of roles in redox balancing during photosynthesis
Ferguson, S. J., JACKSON, J. B., & McEwan, A. G. (1987) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1987.tb02455.x · Cited by 166 · see citing works
The high resolution crystal structure of DMSO reductase in complex with DMSO 1 1Edited by D. C. Rees
McAlpine, A. S., McEwan, A. G., & Bailey, S. L. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1513 · Cited by 165 · see citing works
Chrysiogenes arsenatis gen. nov., sp. nov., a New Arsenate-Respiring Bacterium Isolated from Gold Mine Wastewater
MACY, J. M., NUNAN, K., HAGEN, K. D., DIXON, D. R., HARBOUR, P. J., CAHILL, M., & SLY, L. I. (1996) · International Journal of Systematic Bacteriology · doi:10.1099/00207713-46-4-1153 · Cited by 164 · see citing works
Purification and Molecular Characterization ofortho-Chlorophenol Reductive Dehalogenase, a Key Enzyme of Halorespiration in Desulfitobacterium dehalogenans
van de Pas, B. A., Smidt, H., Hagen, W. R., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.29.20287 · Cited by 164 · see citing works
Reductive dechlorination of 3-chlorobenzoate is coupled to ATP production and growth in an anaerobic bacterium, strain DCB-1
Dolfing, J. (1990) · Archives of Microbiology · doi:10.1007/bf00249079 · Cited by 161 · see citing works
Competition between Escherichia coli strains expressing either a periplasmic or a membrane-bound nitrate reductase: does Nap confer a selective advantage during nitrate-limited growth?
POTTER, L. C., MILLINGTON, P., GRIFFITHS, L., THOMAS, G. H., & COLE, J. A. (1999) · Biochemical Journal · doi:10.1042/0264-6021:3440077 · Cited by 160 · see citing works
Structural and mechanistic mapping of a unique fumarate reductase.
Walkinshaw, M. D., Taylor, P., Pealing, S. L., Reid, G. A., & Chapman, S. K. (1999) · Nature Structural Biology · doi:10.1038/70045 · Cited by 159 · see citing works
A seven‐gene operon essential for formate‐dependent nitrite reduction to ammonia by enteric bacteria
Hussain, H. A., Grove, J. I., Griffiths, L., Busby, S. J. W., & Cole, J. A. (1994) · Molecular Microbiology · doi:10.1111/j.1365-2958.1994.tb01004.x · Cited by 156 · see citing works
Purification and initial kinetic and spectroscopic characterization of NO reductase from Paracoccus denitrificans
Girsch, P., & de Vries, S. (1997) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(96)00138-7 · Cited by 152 · see citing works
Structure and mechanism of the flavocytochrome c fumarate reductase of Shewanella putrefaciens MR-1.
BEEUMEN, J. V., Leys, D., Tsapin, A. S., Nealson, K. H., Meyer, T. E., & Cusanovich, M. A. (1999) · Nature Structural Biology · doi:10.1038/70051 · Cited by 151 · see citing works
The hmc operon of Desulfovibrio vulgaris subsp. vulgaris Hildenborough encodes a potential transmembrane redox protein complex
Rossi, M., Pollock, W. B. R., Reij, M. W., et al. (1993) · Journal of Bacteriology · doi:10.1128/jb.175.15.4699-4711.1993 · Cited by 143 · see citing works
The nirSTBM region coding for cytochrome cd1‐dependent nitrite respiration of Pseudomonas stutzeri consists of a cluster of mono‐, di‐, and tetraheme proteins
Jüngst, A., Wakabayashi, S., Matsubara, H., & Zumft, W. G. (1991) · FEBS Letters · doi:10.1016/0014-5793(91)80150-2 · Cited by 141 · see citing works
Selenium-Containing Formate Dehydrogenase H from Escherichia coli: A Molybdopterin Enzyme That Catalyzes Formate Oxidation without Oxygen Transfer
Khangulov, S. V., Gladyshev, V. N., Dismukes, G. C., & Stadtman, T. C. (1998) · Biochemistry · doi:10.1021/bi972177k · Cited by 141 · see citing works
Outer membrane cytochromes of Shewanella putrefaciens MR-1: spectral analysis, and purification of the 83-kDa c-type cytochrome
Myers, C. R., & Myers, J. M. (1997) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/s0005-2736(97)00034-5 · Cited by 141 · see citing works
Sequence analysis of subunits of the membrane‐bound nitrate reductase from a denitrifying bacterium: the integral membrane subunit provides a prototype for the dihaem electron‐carrying arm of a redox loop
Berks, B. C., Page, M. D., Richardson, D. J., Reilly, A., Cavill, A., Outen, F., & Ferguson, S. J. (1995) · Molecular Microbiology · doi:10.1111/j.1365-2958.1995.tb02246.x · Cited by 140 · see citing works
Self-citation
The napEDABC gene cluster encoding the periplasmic nitrate reductase system of Thiosphaera pantotropha
Berks, B. C., Richardson, D. J., Reilly, A., Willis, A. C., & Ferguson, S. J. (1995) · Biochemical Journal · doi:10.1042/bj3090983 · Cited by 138 · see citing works
Self-citation
The napF and narG Nitrate Reductase Operons in Escherichia coli Are Differentially Expressed in Response to Submicromolar Concentrations of Nitrate but Not Nitrite
Wang, H., Tseng, C., & Gunsalus, R. P. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.17.5303-5308.1999 · Cited by 137 · see citing works
Erratum: The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus
Klenk, H., Clayton, R. A., Tomb, J.-F., White, O. R., Nelson, K. E., Ketchum, K. A., Dodson, R. J., Gwinn, M. L., Hickey, E. K., Peterson, J. D., et al. (1998) · Nature · doi:10.1038/27963 · Cited by 137 · see citing works
Self-citation
Nitric oxide in bacteria: synthesis and consumption
Watmough, N. J., Butland, G. P., Cheesman, M. R., MOIR, J. W. B., Richardson, D. J., & Spiro, S. (1999) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(99)00032-8 · Cited by 136 · see citing works
Self-citation
Purification and some properties of sulfur:ferric ion oxidoreductase from Thiobacillus ferrooxidans
Sugio, T., Mizunashi, W., Kenji Inagaki, Z., & Tano, T. (1987) · Journal of Bacteriology · doi:10.1128/jb.169.11.4916-4922.1987 · Cited by 132 · see citing works
The Periplasmic Nitrate Reductase in Pseudomonas sp. Strain G-179 Catalyzes the First Step of Denitrification
Bedzyk, L. A., Wang, T., & Ye, R. W. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.9.2802-2806.1999 · Cited by 127 · see citing works
Spectroscopic Characterization of a Novel Multihemec-Type Cytochrome Widely Implicated in Bacterial Electron Transport
Roldán, M. D., Sears, H. J., Cheesman, M. R., Ferguson, S. J., THOMSON, A. J., Berks, B. C., & Richardson, D. J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.44.28785 · Cited by 124 · see citing works
Self-citation
The Active Site of the Bacterial Nitric Oxide Reductase Is a Dinuclear Iron Center
Hendriks, J. H. M., Warne, T., Gohlke, U., Haltia, T., Ludovici, C., Lübben, M., & Saraste, M. (1998) · Biochemistry · doi:10.1021/bi980943x · Cited by 123 · see citing works
The terminal oxidases of Paracoccus denitrificans
de Gier, J. L., Lübben, M., Reijnders, W. N. M., et al. (1994) · Molecular Microbiology · doi:10.1111/j.1365-2958.1994.tb00414.x · Cited by 114 · see citing works
Reduction and removal of heptavalent technetium from solution by Escherichia coli
Lloyd, J. R., Cole, J. A., & Macaskie, L. E. (1997) · Journal of Bacteriology · doi:10.1128/jb.179.6.2014-2021.1997 · Cited by 111 · see citing works
Purification and Magneto-optical Spectroscopic Characterization of Cytoplasmic Membrane and Outer Membrane Multiheme c-Type Cytochromes from Shewanella frigidimarina NCIMB400
Field, S. J., Dobbin, P. S., Cheesman, M. R., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.12.8515 · Cited by 111 · see citing works
Heme packing motifs revealed by the crystal structure of the tetra-heme cytochrome c554 from Nitrosomonas europaea
Iverson, T. M., Arciero, D. M., Hsu, B. T., et al. (1998) · Nature Structural Biology · doi:10.1038/2975 · Cited by 110 · see citing works
The role of auxiliary oxidants in maintaining redox balance during phototrophic growth of Rhodobacter capsulatus on propionate or butyrate
Richardson, D. J., King, G. F., Kelly, D. J., McEwan, A. G., Ferguson, S. J., & JACKSON, J. B. (1988) · Archives of Microbiology · doi:10.1007/bf00425152 · Cited by 105 · see citing works
Self-citation
Reduction of nitrate to nitrite by molybdenum-mediated atom transfer: a nitrate reductase analog reaction system
Craig, J. A., & Holm, R. H. (1989) · Journal of the American Chemical Society · doi:10.1021/ja00188a026 · Cited by 101 · cited 1× · see citing works
“Thus, for example, some can exhibit both nitrate reductase and DMSO reductase activity (Craig & Holm, 1989).”
Background
Models for Molybdenum Coordination during the Catalytic Cycle of Periplasmic Nitrate Reductase from Paracoccus denitrificans Derived from EPR and EXAFS Spectroscopy
Butler, C. S., Charnock, J. M., Bennett, B., Sears, H. J., Reilly, A. J., Ferguson, S. J., Garner, C. D., Lowe, D. J., Thomson, A. J., Berks, B. C., et al. (1999) · Biochemistry · doi:10.1021/bi990402n · Cited by 99 · see citing works
Self-citation
Regulation and sequence of the structural gene for cytochrome C552 from Escherichia coli: not a hexahaem but a 50kDa tetrahaem nitrite reductase
Darwin, A. J., Hussain, H. A., Griffiths, L., Grove, J. I., Sambongi, Y., Busby, S. J. W., & Cole, J. A. (1993) · Molecular Microbiology · doi:10.1111/j.1365-2958.1993.tb01255.x · Cited by 99 · see citing works
The influence of carbon substrate on the activity of the periplasmic nitrate reductase in aerobically grown Thiosphaera pantotropha
Richardson, D. J., & Ferguson, S. J. (1992) · Archives of Microbiology · doi:10.1007/bf00276774 · Cited by 97 · see citing works
Self-citation
A Low-Redox Potential Heme in the Dinuclear Center of Bacterial Nitric Oxide Reductase: Implications for the Evolution of Energy-Conserving Heme−Copper Oxidases
Grönberg, K. L. C., Roldán, M. D., Prior, L., et al. (1999) · Biochemistry · doi:10.1021/bi9916426 · Cited by 97 · see citing works
Detection of genes for periplasmic nitrate reductase in nitrate respiring bacteria and in community DNA
Flanagan, D., Gregory, L. G., Carter, J. P., Karakas-Sen, A., Richardson, D. J., & Spiro, S. (1999) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1999.tb13742.x · Cited by 97 · see citing works
Self-citation
Cloning, sequencing, and expression of the gene encoding the high-molecular-weight cytochrome c from Desulfovibrio vulgaris Hildenborough
Pollock, W. B. R., Loutfi, M., Bruschi, M., et al. (1991) · Journal of Bacteriology · doi:10.1128/jb.173.1.220-228.1991 · Cited by 95 · see citing works
Isolation and sequence of omcA , a gene encoding a decaheme outer membrane cytochrome c of Shewanella putrefaciens MR-1, and detection of omcA homologs in other strains of S. putrefaciens
Myers, J. M., & Myers, C. R. (1998) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/s0005-2736(98)00111-4 · Cited by 95 · see citing works
Impact of either Elevated or Decreased Levels of Cytochrome bd Expression on Shigella flexneri Virulence
Way, S. S., Sallustio, S., Magliozzo, R. S., & Goldberg, M. B. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.4.1229-1237.1999 · Cited by 94 · see citing works
Essential roles for the products of the napABCD genes, but not napFGH, in periplasmic nitrate reduction by Escherichia coli K-12
POTTER, L. C., & COLE, J. A. (1999) · Biochemical Journal · doi:10.1042/0264-6021:3440069 · Cited by 93 · see citing works
Optical Biosensing of Nitrate Ions Using a Sol–Gel Immobilized Nitrate Reductase
Aylott, J. W., Richardson, D. J., & Russell, D. A. (1997) · The Analyst · doi:10.1039/a606146j · Cited by 90 · see citing works
Self-citation
Multiple States of the Molybdenum Centre of Dimethylsulphoxide Reductase from Rhodobacter Capsulatus Revealed by EPR Spectroscopy
Bennett, B., Benson, N., McEwan, A. G., & Bray, R. C. (1994) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1994.00321.x · Cited by 86 · see citing works
The rpoS-dependent starvation-stress response locus stiA encodes a nitrate reductase (narZYWV) required for carbon-starvation-inducible thermotolerance and acid tolerance in Salmonella typhimurium
Spector, M. P., del Portillo, F. G., Bearson, S. M. D., Mahmud, A., Magut, M., Finlay, B. B., Gordon Dougan, B., Foster, J. W., & Pallen, M. J. (1999) · Microbiology · doi:10.1099/00221287-145-11-3035 · Cited by 86 · see citing works
Nitrate and Nitrite Utilization in Sulfate-Reducing Bacteria
Moura, I., Bursakov, S. A., Costa, C., & Moura, J. J. G. (1997) · Anaerobe · doi:10.1006/anae.1997.0093 · Cited by 84 · see citing works
Enzymatic and physiological properties of the tungsten‐substituted molybdenum TMAO reductase from Escherichia coli
Buc, J., Santini, C., Giordani, R., Czjzek, M., Wu, L., & Giordano, G. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01340.x · Cited by 83 · see citing works
The diversity of redox proteins involved in bacterial heterotrophic nitrification and aerobic denitrification
Richardson, D. J., Wehrfritz, J.-M., Keech, A. M., et al. (1998) · Biochemical Society Transactions · doi:10.1042/bst0260401 · Cited by 81 · see citing works
Self-citation
Purification and characterization of the single‐component nitric oxide reductase from Ralstonia eutropha H16
Cramm, R., Pohlmann, A., & Friedrich, B. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01315-0 · Cited by 78 · see citing works
Respiratory Chains in the Last Common Ancestor of Living Organisms
Castresana, J., & Moreira, D. (1999) · Journal of Molecular Evolution · doi:10.1007/pl00006568 · Cited by 77 · see citing works
Identification of nitric oxide reductase activity in Rhodobacter capsulatus: the electron transport pathway can either use or bypass both cytochrome c2 and the cytochrome bc1 complex
Bell, L. C., Richardson, D. J., & Ferguson, S. J. (1992) · Journal of General Microbiology · doi:10.1099/00221287-138-3-437 · Cited by 76 · see citing works
Self-citation
cis - and trans -Acting Elements Involved in Regulation of aniA , the Gene Encoding the Major Anaerobically Induced Outer Membrane Protein in Neisseria gonorrhoeae
Householder, T. C., Belli, W. A., Lissenden, S., et al. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.2.541-551.1999 · Cited by 76 · see citing works
Bioenergetics of sulphate-reducing bacteria in relation to their environmental impact
Hamilton, W. A. (1998) · Biodegradation · doi:10.1023/a:1008362304234 · Cited by 75 · see citing works
Open conformation of a flavocytochrome c3 fumarate reductase.
Hemmings, A. M., Bamford, V. A., Dobbin, P. S., & Richardson, D. J. (1999) · Nature Structural Biology · doi:10.1038/70039 · Cited by 75 · see citing works
Self-citation
Organization of the hao gene cluster of Nitrosomonas europaea: genes for two tetraheme c cytochromes
Bergmann, D., Arciero, D. M., & Hooper, A. B. (1994) · Journal of Bacteriology · doi:10.1128/jb.176.11.3148-3153.1994 · Cited by 75 · see citing works
Molybdenum Cofactor Properties and [Fe-S] Cluster Coordination in Escherichia coli Nitrate Reductase A: Investigation by Site-Directed Mutagenesis of the Conserved His-50 Residue in the NarG Subunit
Magalon, A., Asso, M., Guigliarelli, B., Rothery, R. A., Bertrand, P., Giordano, G., & Blasco, F. (1998) · Biochemistry · doi:10.1021/bi972858f · Cited by 75 · see citing works
Sulfonates as Terminal Electron Acceptors for Growth of Sulfite-Reducing Bacteria (Desulfitobacteriumspp.) and Sulfate-Reducing Bacteria: Effects of Inhibitors of Sulfidogenesis
Lie, T. J., Godchaux, W., & Leadbetter, E. R. (1999) · Applied and Environmental Microbiology · doi:10.1128/aem.65.10.4611-4617.1999 · Cited by 74 · see citing works
Fast Cytochrome bo from Escherichia coli Binds Two Molecules of Nitric Oxide at CuB
Butler, C. S., Seward, H. E., Greenwood, C., et al. (1997) · Biochemistry · doi:10.1021/bi971481a · Cited by 74 · see citing works
Characterization of a flavocytochrome that is induced during the anaerobic respiration of Fe3+ by Shewanella frigidimarina NCIMB400
Dobbin, P. S., Butt, J. N., Powell, A. K., REID, G. A., & Richardson, D. J. (1999) · Biochemical Journal · doi:10.1042/bj3420439 · Cited by 73 · see citing works
Self-citation
The primary and three-dimensional structures of a nine-haem cytochrome c from Desulfovibrio desulfuricans ATCC 27774 reveal a new member of the Hmc family
Matias, P. M., Coelho, R., Pereira, I. A. C., et al. (1999) · Structure · doi:10.1016/s0969-2126(99)80019-7 · Cited by 72 · see citing works
Two isofunctional nitric oxide reductases in Alcaligenes eutrophus H16
Cramm, R., Siddiqui, R. A., & Friedrich, B. (1997) · Journal of Bacteriology · doi:10.1128/jb.179.21.6769-6777.1997 · Cited by 72 · see citing works
Nitrate and Nitrite Regulation of the Fnr-dependentaeg-46.5Promoter ofEscherichia coliK-12 is Mediated by Competition Between Homologous Response Regulators (NarL and NarP) for a Common DNA-binding Site
Darwin, A. J., & Stewart, V. J. (1995) · Journal of Molecular Biology · doi:10.1006/jmbi.1995.0412 · Cited by 71 · see citing works
On the origin of respiration: electron transport proteins from archaea to man
Schäfer, G., Purschke, W. G., & Schmidt, C. L. (1996) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.1996.tb00235.x · Cited by 65 · see citing works
The identification of a periplasmic nitrate reductase in Paracoccus denitrificans
Sears, H. J., Ferguson, S. J., Richardson, D. J., & Spiro, S. (1993) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1993.tb06496.x · Cited by 64 · see citing works
Self-citation
Essential roles for the products of the napABCD genes, but not napFGH, in periplasmic nitrate reduction by Escherichia coli K-12
POTTER, L. C., & Cole, J. A. (1999) · Biochemical Journal · doi:10.1042/bj3440069 · Cited by 63 · see citing works
Evidence for a Chemiosmotic Model of Dehalorespiration in Desulfomonile tiedjei DCB-1
Louie, T. M., & Mohn, W. W. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.1.40-46.1999 · Cited by 61 · see citing works
Mo(V) Electron Paramagnetic Resonance Signals from the Periplasmic Nitrate Reductase of Thiosphaera Pantotropha
Bennett, B., Berks, B. C., Ferguson, S. J., Thomson, A. J., & Richardson, D. J. (1994) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1994.00789.x · Cited by 58 · see citing works
Self-citation
Cu A and Cu Z are variants of the electron transfer center in nitrous oxide reductase
Farrar, J. A., Zumft, W. G., & Thomson, A. J. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.17.9891 · Cited by 57 · see citing works
Re-design of Rhodobacter sphaeroides Dimethyl Sulfoxide Reductase
Hilton, J. C., Temple, C. A., & Rajagopalan, K. V. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.13.8428 · Cited by 56 · see citing works
Periplasmic nitrate-reducing system of the phototrophic bacterium Rhodobacter sphaeroides DSM 158: transcriptional and mutational analysis of the napKEFDABC gene cluster
REYES, F., GAVIRA, M., CASTILLO, F., & MORENO-VIVIÁN, C. (1998) · Biochemical Journal · doi:10.1042/bj3310897 · Cited by 56 · see citing works
Dissimilatory iron(III) reduction by Rhodobacter capsulatus
Dobbin, P. S., Warren, L. H., Cook, N., et al. (1996) · Microbiology · doi:10.1099/00221287-142-4-765 · Cited by 55 · see citing works
Effect of carbon substrate and aeration on nitrate reduction and expression of the periplasmic and membrane-bound nitrate reductases in carbon-limited continuous cultures of Paracoccus denitrificans Pd1222
Sears, H. J., Spiro, S. G., & Richardson, D. J. (1997) · Microbiology · doi:10.1099/00221287-143-12-3767 · Cited by 54 · see citing works
Self-citation
The biochemical characterization of a novel non-haem-iron hydroxylamine oxidase from Paracoccus denitrificans GB17
MOIR, J. W. B., Wehrfritz, J.-M., Spiro, S. G., et al. (1996) · Biochemical Journal · doi:10.1042/bj3190823 · Cited by 54 · see citing works
Characterization of DorC from Rhodobacter capsulatus, a c-type Cytochrome Involved in Electron Transfer to Dimethyl Sulfoxide Reductase
Shaw, A. L., Hochkoeppler, A., Bonora, P., Zannoni, D., Hanson, G. R., & McEwan, A. G. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.15.9911 · Cited by 52 · see citing works
The Dinuclear Center of Cytochrome bo 3 from Escherichia coli
Watmough, N. J., Cheesman, M. R., Butler, C. S., et al. (1998) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1020507511285 · Cited by 46 · see citing works
The Hemes of Escherichia coli Nitrate Reductase A (NarGHI): Potentiometric Effects of Inhibitor Binding to NarI
Rothery, R. A., Blasco, F., Magalon, A., Asso, M., & Weiner, J. H. (1999) · Biochemistry · doi:10.1021/bi990533o · Cited by 46 · see citing works
Purification and some properties of sulfite:ferric ion oxidoreductase from Thiobacillus ferrooxidans
Sugio, T., Hirose, T., Ye, L. Z., et al. (1992) · Journal of Bacteriology · doi:10.1128/jb.174.12.4189-4192.1992 · Cited by 44 · see citing works
Refinement of the three-dimensional structures of cytochrome c3 from Desulfovibrio vulgaris Hildenborough at 1.67 Å resolution and from Desulfovibrio desulfuricans ATCC 27774 at 1.6 Å resolution
Simões, P. N., Matias, P. M., Morais, J., et al. (1998) · Inorganica Chimica Acta · doi:10.1016/s0020-1693(97)06018-0 · Cited by 43 · see citing works
The role of auxiliary oxidants in the maintenance of a balanced redox poise for photosynthesis in bacteria
McEwan, A. G., COTTON, N. P. J., Ferguson, S. J., et al. (1985) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(85)90129-x · Cited by 39 · see citing works
Involvement in Denitrification of thenapKEFDABCGenes Encoding the Periplasmic Nitrate Reductase System in the Denitrifying Phototrophic BacteriumRhodobacter sphaeroidesf. sp.denitrificans
Hui-Ping, L. I. U., Takio, S., Satoh, T., & Yamamoto, I. (1999) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.63.530 · Cited by 37 · see citing works
The influence of chelating agents upon the dissimilatory reduction of Fe(III) by Shewanella putrefaciens
Dobbin, P. S., Powell, A. K., McEwan, A. G., & Richardson, D. J. (1995) · BioMetals · doi:10.1007/bf00142016 · Cited by 36 · see citing works
Self-citation
In vivo redox poising of the cyclic electron transport system of Rhodobacter capsulatus and the effects of the auxiliary oxidants, nitrate, nitrous oxide and trimethylamine N-oxide, as revealed by multiple short flash excitation
Jones, M. R., Richardson, D. J., McEwan, A. G., et al. (1990) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(90)90186-8 · Cited by 32 · see citing works
Self-citation
Isolation and nucleotide sequence of the gene (aniA) encoding the major anaerobically induced outer membrane protein of Neisseria gonorrhoeae
Hoehn, G., & Clark, V. L. (1992) · Infection and Immunity · doi:10.1128/iai.60.11.4695-4703.1992 · Cited by 32 · see citing works
Identification of an assimilatory nitrate reductase in mutants of Paracoccus denitrificans GB17 deficient in nitrate respiration
Sears, H. J., Little, P. J., Richardson, D. J., Berks, B. C., Spiro, S., & Ferguson, S. J. (1997) · Archives of Microbiology · doi:10.1007/s002030050417 · Cited by 31 · see citing works
Self-citation
Molecular and Regulatory Properties of the Nitrate Reducing Systems of Rhodobacter
del Castillo, F. J., Dobao, M. M., Reyes, F., Blasco, R., Roldán, M. D., Gavira, M., F.J. Caballero, & Martínez‐Luque, M. (1996) · Current Microbiology · doi:10.1007/s002849900125 · Cited by 30 · see citing works
Expression of glnB and a glnB -Like Gene ( glnK ) in a Ribulose Bisphosphate Carboxylase/Oxygenase-Deficient Mutant of Rhodobacter sphaeroides
Qian, Y., & Tabita, F. R. (1998) · Journal of Bacteriology · doi:10.1128/jb.180.17.4644-4649.1998 · Cited by 29 · see citing works
Transcriptional control and essential roles of the Escherichia coli ccm gene products in formate-dependent nitrite reduction and cytochrome c synthesis
Tanapongpipat, S., Reid, E. G. F., Cole, J. A., & Crooke, H. (1998) · Biochemical Journal · doi:10.1042/bj3340355 · Cited by 25 · see citing works
Structure and evolution of cytochrome oxidase
Saraste, M. (1994) · Antonie van Leeuwenhoek · doi:10.1007/bf00872214 · Cited by 25 · see citing works
Structural investigation of the molybdenum site of the periplasmic nitrate reductase from Thiosphaera pantotropha by X-ray absorption spectroscopy
Bennett, B., Charnock, J., Sears, H. J., Berks, B. C., THOMSON, A. J., Ferguson, S. J., Garner, C. D., & RICHARDSON, D. J. (1996) · Biochemical Journal · doi:10.1042/bj3170557 · Cited by 20 · see citing works
Self-citation
Restoration of the optimal redox state for the photosynthetic electron transfer system by auxiliary oxidants in an aerobic photosynthetic bacterium, Erythrobacter sp. OCh 114
Takamiya, K. I., Arata, H., Shioi, Y., et al. (1988) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(88)90104-1 · Cited by 20 · see citing works
The influence of chelating agents upon the dissimilatory reduction of Fe(III) byShewanella putrefaciens. Part 2. Oxo-and hydroxo-bridged polynuclear Fe(III) complexes
Dobbin, P. S., Burmeister, L. M. R., Heath, S. L., Powell, A. K., McEwan, A. G., & Richardson, D. J. (1996) · BioMetals · doi:10.1007/bf00817930 · Cited by 13 · see citing works
Self-citation
CRYSTAL STRUCTURE OF THE FLAVOCYTOCHROME C FUMARATE REDUCTASE OF SHEWANELLA PUTREFACIENS STRAIN MR-1 COMPLEXED WITH FUMARATE
Leys, D., Tsapin, A. S., Meyer, T. E., et al. (1999) · Worldwide Protein Data Bank · doi:10.2210/pdb1d4e/pdb · Cited by 6 · see citing works

Flagged first, then by citations

Sorted by citations

Nitrate and periplasmic nitrate reductases
Sparacino-Watkins, C., Stolz, J. F., & Basu, P. (2014) · Chem. Soc. Rev. · doi:10.1039/c3cs60249d · Cited by 426 · see citing works
Enzymology and bioenergetics of respiratory nitrite ammonification
Simon, J. (2002) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2002.tb00616.x · Cited by 403 · see citing works
A Sterol-Regulatory Element Binding Protein Is Required for Cell Polarity, Hypoxia Adaptation, Azole Drug Resistance, and Virulence in Aspergillus fumigatus
Willger, S. D., Puttikamonkul, S., Kim, K.-H., Burritt, J. B., Grahl, N., Metzler, L. J., Barbuch, R., Bard, M., Lawrence, C. B., & Cramer, R. A. (2008) · PLoS Pathogens · doi:10.1371/journal.ppat.1000200 · Cited by 345 · see citing works
Roles of NapF, NapG and NapH, subunits of the Escherichia coli periplasmic nitrate reductase, in ubiquinol oxidation: Roles of NapF, G and H in ubiquinol oxidation in E. coli
Brondijk, T. H. C., Fiegen, D., Richardson, D. J., & Cole, J. A. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.02875.x · Cited by 342 · see citing works
Self-citation
Changes in energy metabolism of Mycobacterium tuberculosis in mouse lung and under in vitro conditions affecting aerobic respiration
Shi, L., Sohaskey, C. D., Kana, B. D., Dawes, S., North, R. J., Mizrahi, V., & Gennaro, M. L. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0507850102 · Cited by 301 · see citing works
Cytochrome c Biogenesis: Mechanisms for Covalent Modifications and Trafficking of Heme and for Heme-Iron Redox Control
Kranz, R. G., Richard-Fogal, C., Taylor, J.-S., & Frawley, E. R. (2009) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00001-09 · Cited by 275 · see citing works
Aerobic Respiration Metabolism in Lactic Acid Bacteria and Uses in Biotechnology
Pedersen, M. B., Gaudu, P., Lechardeur, D., Petit, M.-A., & Gruss, A. (2012) · Annual Review of Food Science and Technology · doi:10.1146/annurev-food-022811-101255 · Cited by 197 · see citing works
Protective effect of salivary nitrate and microbial nitrate reductase activity against caries
Doel, J. J., Hector, M. P., Amirtham, C. V., Al‐Anzan, L. A., Benjamin, N., & Allaker, R. P. (2004) · European Journal Of Oral Sciences · doi:10.1111/j.1600-0722.2004.00153.x · Cited by 131 · see citing works
Periplasmic nitrate reductase revisited: a sulfur atom completes the sixth coordination of the catalytic molybdenum
Najmudin, S., González, P. J., Trincão, J., Coelho, C., Mukhopadhyay, A., Cerqueira, N. M. F. S. A., Romão, C. C., Moura, I., Moura, J. J. G., Brondino, C. D., et al. (2008) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-008-0359-6 · Cited by 116 · see citing works
Nitrous Oxide Metabolism in Nitrate-Reducing Bacteria
(2016) · Advances in Microbial Physiology · doi:10.1016/bs.ampbs.2016.02.007 · Cited by 100 · see citing works
Nitrate, nitrite and nitric oxide reductases: from the last universal common ancestor to modern bacterial pathogens
Vázquez-Torres, A., & Bäumler, A. J. (2016) · Current Opinion in Microbiology · doi:10.1016/j.mib.2015.09.002 · Cited by 92 · see citing works
Voltammetric Studies of the Catalytic Mechanism of the Respiratory Nitrate Reductase from Escherichia coli: How Nitrate Reduction and Inhibition Depend on the Oxidation State of the Active Site
Elliott, S. J., Hoke, K. R., Heffron, K., Palak, M., Rothery, R. A., Weiner, J. H., & Armstrong, F. A. (2004) · Biochemistry · doi:10.1021/bi035869j · Cited by 90 · see citing works
Multivariate regulation of soil CO2 and N2O pulse emissions from agricultural soils
Liang, L. L., Grantz, D. A., & Jenerette, G. D. (2016) · Global Change Biology · doi:10.1111/gcb.13130 · Cited by 78 · see citing works
The CcmC:Heme:CcmE Complex in Heme Trafficking and Cytochrome c Biosynthesis
Richard-Fogal, C., & Kranz, R. G. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.06.041 · Cited by 53 · see citing works
EPR and redox properties of periplasmic nitrate reductase from Desulfovibrio desulfuricans ATCC 27774
González, P. J., Rivas, M. G., Brondino, C. D., Bursakov, S. A., Moura, I., & Moura, J. J. G. (2006) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-006-0110-0 · Cited by 45 · see citing works
Identification of two domains and distal histidine ligands to the four haems in the bacterial c-type cytochrome NapC; the prototype connector between quinol/quinone and periplasmic oxido-reductases
CARTRON, M. L., ROLDÁN, M. D., FERGUSON, S. J., BERKS, B. C., & RICHARDSON, D. J. (2002) · Biochemical Journal · doi:10.1042/bj20020865 · Cited by 43 · see citing works
Self-citation
Substrate-dependent modulation of the enzymatic catalytic activity: Reduction of nitrate, chlorate and perchlorate by respiratory nitrate reductase from Marinobacter hydrocarbonoclasticus 617
Marangon, J., Paes de Sousa, P. M., Moura, I., Brondino, C. D., Moura, J. J. G., & González, P. J. (2012) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2012.04.011 · Cited by 40 · see citing works
Role of a Conserved Glutamine Residue in Tuning the Catalytic Activity of Escherichia coli Cytochrome c Nitrite Reductase
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 · see citing works
Self-citation
Periplasmic nitrate reduction in Wolinella succinogenes: cytoplasmic NapF facilitates NapA maturation and requires the menaquinol dehydrogenase NapH for membrane attachment
Kern, M., & Simon, J. (2009) · Microbiology · doi:10.1099/mic.0.029983-0 · Cited by 33 · see citing works
Adaptation to a High-Tungsten Environment: Pyrobaculum aerophilum Contains an Active Tungsten Nitrate Reductase
de Vries, S., Momcilovic, M., Strampraad, M. J. F., Whitelegge, J. P., Baghai, A., & Schröder, I. (2010) · Biochemistry · doi:10.1021/bi100974v · Cited by 29 · see citing works

Authors: Richardson, D. J.
Affiliations: University of East Anglia (GB)
Corresponding author: Richardson, David J.
ORCID: Richardson, David J.
Venue: Microbiology
Publisher: Microbiology Society
Published: 2000-03-01
Volume: 146
Issue: 3
Pages: 551-571
ISSN: 1350-0872 (ISSN-L)
1465-2080
DOI: 10.1099/00221287-146-3-551
OpenAlex: W1851503055
Cited by: 544
References: 139
Citations by year: 2026: 13 · 2025: 20 · 2024: 12 · 2023: 13 · 2022: 12 · 2021: 19 · 2020: 21 · 2019: 18 · 2018: 26 · 2017: 13 · 2016: 24 · 2015: 24 · 2014: 26 · 2013: 28 · 2012: 34
FWCI: 2.28
Type: journal article
Language: en
Open access: closed
Locations: Microbiology (publishedVersion)
PubMed (publishedVersion)
UEA Digital Repository (University of East Anglia) (submittedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Microbial metabolism and enzyme function
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Keywords: bacterial respiration, respiratory metabolism, metabolic flexibility, environmental adaptation, bacterial physiology
MeSH terms: Amino Acid Sequence, Bacteria, Cytochrome c Group, Ferric Compounds, Molecular Sequence Data, Nitrate Reductases, Nitrates, Oxidation-Reduction, Oxidoreductases, Oxygen Consumption

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Bacterial respiration: a flexible process for a changing environment 1999 Fleming Lecture (Delivered at the 144th meeting of the Society for General Microbiology, 8 September 1999)

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Cites

Cited by

Related

Record

About these checks