Richardson, David J.

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, D. J. (2000) · Microbiology

Bacterial Genetics and BiotechnologyMicrobial metabolism and enzyme function

Cited by 544

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

Bacterial Genetics and BiotechnologyMetalloenzymes and iron-sulfur proteins

Cited by 342

Nitrate reduction in the periplasm of gram-negative bacteria

Potter, L., Angove, H., Richardson, D., & Cole, J. (2001) · Advances in Microbial Physiology

Bacterial Genetics and BiotechnologyMetalloenzymes and iron-sulfur proteins

Cited by 152

Spectropotentiometric and Structural Analysis of the Periplasmic Nitrate Reductase from Escherichia coli

Jepson, B. J. N., Mohan, S., Clarke, T. A., Gates, A. J., Cole, J. A., Butler, C. S., Butt, J. N., Hemmings, A. M., & Richardson, D. J. (2007) · Journal of Biological Chemistry

Metalloenzymes and iron-sulfur proteinsEnzyme Structure and Function

Cited by 120

Catalytic Protein Film Voltammetry from a Respiratory Nitrate Reductase Provides Evidence for Complex Electrochemical Modulation of Enzyme Activity

Anderson, L. J., Richardson, D. J., & Butt, J. N. (2001) · Biochemistry

Metalloenzymes and iron-sulfur proteinsElectrochemical sensors and biosensors

Cited by 113

Nitrous Oxide Metabolism in Nitrate-Reducing Bacteria

Torres, M. J., Simon, J., Rowley, G., Bedmar, E. J., Richardson, D. J., Gates, A. J., & Delgado, M. J. (2016) · Advances in Microbial Physiology

Soil Carbon and Nitrogen DynamicsWastewater Treatment and Nitrogen Removal

Cited by 100

NapGH components of the periplasmic nitrate reductase of Escherichia coli K-12: location, topology and physiological roles in quinol oxidation and redox balancing

BRONDIJK, T. H. C., NILAVONGSE, A., FILENKO, N., RICHARDSON, D. J., & COLE, J. A. (2004) · Biochemical Journal

Bacterial Genetics and BiotechnologyMetalloenzymes and iron-sulfur proteins

Cited by 87

Control of periplasmic nitrate reductase gene expression (napEDABC) from Paracoccus pantotrophus in response to oxygen and carbon substrates

Sears, H. J., Sawers, G., Berks, B. C., Ferguson, S. J., & Richardson, D. J. (2000) · Microbiology

Bacterial Genetics and BiotechnologyWastewater Treatment and Nitrogen Removal

Cited by 76

Structural diversity in twin-arginine signal peptide-binding proteins

Maillard, J., Spronk, C. A. E. M., Buchanan, G., Lyall, V., Richardson, D. J., Palmer, T., Vuister, G. W., & Sargent, F. (2007) · Proceedings of the National Academy of Sciences

Bacterial Genetics and BiotechnologyEnzyme Structure and Function

Cited by 74

Nitrate reduction by Desulfovibrio desulfuricans: A periplasmic nitrate reductase system that lacks NapB, but includes a unique tetraheme c-type cytochrome, NapM

Marietou, A., Richardson, D., Cole, J., & Mohan, S. (2005) · FEMS Microbiology Letters

Microbial Fuel Cells and BioremediationMetalloenzymes and iron-sulfur proteins

Cited by 68

The NapF protein of the Escherichia coli periplasmic nitrate reductase system: demonstration of a cytoplasmic location and interaction with the catalytic subunit, NapA

Nilavongse, A., Brondijk, T. H. C., Overton, T. W., Richardson, D. J., Leach, E. R., & Cole, J. A. (2006) · Microbiology

Metalloenzymes and iron-sulfur proteinsBacterial Genetics and Biotechnology

Cited by 54

NapF Is a Cytoplasmic Iron-Sulfur Protein Required for Fe-S Cluster Assembly in the Periplasmic Nitrate Reductase

Olmo-Mira, M. F., Gavira, M., Richardson, D. J., Castillo, F., Moreno-Vivián, C., & Roldán, M. D. (2004) · Journal of Biological Chemistry

Metalloenzymes and iron-sulfur proteinsEnzyme Structure and Function

Cited by 44

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

Metalloenzymes and iron-sulfur proteinsMetal-Catalyzed Oxygenation Mechanisms

Cited by 43

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

Metal-Catalyzed Oxygenation MechanismsMetalloenzymes and iron-sulfur proteins

Cited by 40