Richard Rothery researcher ORCID ID = 0000-0003-3265-1783
Rothery, Richard
VIAF ID: 273271914 (Personal)
Permalink: http://viaf.org/viaf/273271914
Preferred Forms
- 100 0 _ ‡a Richard Rothery ‡c researcher ORCID ID = 0000-0003-3265-1783
-
- 100 1 _ ‡a Rothery, Richard
- 100 1 _ ‡a Rothery, Richard
- 100 1 _ ‡a Rothery, Richard
4xx's: Alternate Name Forms (1)
Works
Title | Sources |
---|---|
The catalytic subunit of Escherichia coli nitrate reductase A contains a novel [4Fe-4S] cluster with a high-spin ground state. | |
Characterization of an Escherichia coli sulfite oxidase homologue reveals the role of a conserved active site cysteine in assembly and function. | |
A conserved lysine residue controls iron-sulfur cluster redox chemistry in Escherichia coli fumarate reductase. | |
The covalent attachment of FAD to the flavoprotein of Saccharomyces cerevisiae succinate dehydrogenase is not necessary for import and assembly into mitochondria | |
Defining the Q-site of Escherichia coli fumarate reductase by site-directed mutagenesis, fluorescence quench titrations and EPR spectroscopy. | |
Detection and interpretation of redox potential optima in the catalytic activity of enzymes | |
Easy method for SDS-PAGE gel drying and preservation. | |
Effects of site-directed mutations in Escherichia coli succinate dehydrogenase on the enzyme activity and production of superoxide radicals. | |
Electrochemical evidence that pyranopterin redox chemistry controls the catalysis of YedY, a mononuclear Mo enzyme | |
Fumarate reductase and succinate oxidase activity of Escherichia coli complex II homologs are perturbed differently by mutation of the flavin binding domain. | |
Heme axial ligation by the highly conserved His residues in helix II of cytochrome b | |
Inhibitor binding within the NarI subunit (cytochrome bnr) of Escherichia coli nitrate reductase A | |
The molybdenum cofactor of Escherichia coli nitrate reductase A (NarGHI). Effect of a mobAB mutation and interactions with [Fe-S] clusters | |
Novel growth characteristics and high rates of nitrate reduction of anEscherichia colistrain, LCB2048, that expresses only a periplasmic nitrate reductase | |
The orientation of the three haems of the 'in situ' ubiquinol oxidase, cytochrome bd, of Escherichia coli | |
Peroxynitrite is a major contributor to cytokine-induced myocardial contractile failure | |
Perturbation of the Quinone-binding Site of Complex II Alters the Electronic Properties of the Proximal [3Fe-4S] Iron-Sulfur Cluster | |
The prokaryotic complex iron-sulfur molybdoenzyme family. | |
Pyranopterin conformation defines the function of molybdenum and tungsten enzymes. | |
The quinone binding site in Escherichia coli succinate dehydrogenase is required for electron transfer to the heme b. | |
The respiratory chain of anaerobically grown Escherichia coli: reactions with nitrite and oxygen | |
Shifting the metallocentric molybdoenzyme paradigm: the importance of pyranopterin coordination. | |
Structural and biochemical characterization of a quinol binding site of Escherichia coli nitrate reductase A. | |
Topological characterization of Escherichia coli DMSO reductase by electron paramagnetic resonance spectroscopy of an engineered [3Fe-4S] cluster. | |
Transient kinetic studies of heme reduction in Escherichia coli nitrate reductase A (NarGHI) by menaquinol. | |
Vehicular traffic science; proceedings | |
X-ray absorption spectroscopic characterization of the molybdenum site of Escherichia coli dimethyl sulfoxide reductase. |