Howes et al., 1997 - Google Patents
Mutation of distal residues of horseradish peroxidase: influence on substrate binding and cavity propertiesHowes et al., 1997
- Document ID
- 5031651716485790952
- Author
- Howes B
- Rodriguez-Lopez J
- Smith A
- Smulevich G
- Publication year
- Publication venue
- Biochemistry
External Links
Snippet
The manner in which the distal heme pocket residues of peroxidases control the reaction mechanism and ligand binding has been investigated further by analysis of the electronic absorption and resonance Raman (RR) spectra of distal site mutants of recombinant …
- 230000027455 binding 0 title abstract description 86
Classifications
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
- G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N21/00—Investigating or analysing materials by the use of optical means, i.e. using infra-red, visible or ultra-violet light
- G01N21/75—Systems in which material is subjected to a chemical reaction, the progress or the result of the reaction being investigated
Similar Documents
Publication | Publication Date | Title |
---|---|---|
Howes et al. | Mutation of distal residues of horseradish peroxidase: influence on substrate binding and cavity properties | |
Hayashi et al. | Peroxidase activity of myoglobin is enhanced by chemical mutation of heme-propionates | |
Hargrove et al. | Structural factors governing hemin dissociation from metmyoglobin | |
Hayashi et al. | Blue myoglobin reconstituted with an iron porphycene shows extremely high oxygen affinity | |
Clay et al. | Spectroscopic studies of Pyrococcus furiosus superoxide reductase: implications for active-site structures and the catalytic mechanism | |
Battistuzzi et al. | Redox thermodynamics of the native and alkaline forms of eukaryotic and bacterial class I cytochromes c | |
Zhao et al. | Identification of histidine 105 in the β1 subunit of soluble guanylate cyclase as the heme proximal ligand | |
Neri et al. | Fluoride binding in hemoproteins: The importance of the distal cavity structure | |
Gibney et al. | Self-assembly of heme A and heme B in a designed four-helix bundle: implications for a cytochrome c oxidase maquette | |
Whittaker et al. | The oxidized (3, 3) state of manganese catalase. Comparison of enzymes from Thermus thermophilus and Lactobacillus plantarum | |
Zhao et al. | Is hydrogen peroxide produced during iron (II) oxidation in mammalian apoferritins? | |
Mulholland et al. | Characterization of the fundamental protein ligand requirements of [4Fe-4S] 2+/+ clusters with sixteen amino acid maquettes | |
Hinchliffe et al. | Identification of a novel subunit of respiratory complex I from Thermus thermophilus | |
Kriegel et al. | Biomimetic environment to study E. coli complex I through surface-enhanced IR absorption spectroscopy | |
Zu et al. | Redox properties of the [2Fe-2S] center in the 24 kDa (NQO2) subunit of NADH: ubiquinone oxidoreductase (complex I) | |
Sezer et al. | Distinct structural and redox properties of the heme active site in bacterial dye decolorizing peroxidase-type peroxidases from two subfamilies: resonance Raman and electrochemical study | |
Tsuno et al. | Interaction and inhibitory effect of ammonium cation in the oxygen evolving center of photosytem II | |
Ojha et al. | Effects of heme ligand mutations including a pathogenic variant, H65R, on the properties of human cystathionine β-synthase | |
Feng et al. | Essential role of conserved arginine 160 in intramolecular electron transfer in human sulfite oxidase | |
Nissum et al. | Spectroscopic characterization of recombinant pea cytosolic ascorbate peroxidase: similarities and differences with cytochrome c peroxidase | |
Heering et al. | New insights into the heme cavity structure of catalase-peroxidase: a spectroscopic approach to the recombinant Synechocystis enzyme and selected distal cavity mutants | |
Indiani et al. | Benzohydroxamic Acid− Peroxidase Complexes: Spectroscopic Characterization of a Novel Heme Spin Species | |
Munter et al. | Model peptides uncover the role of the β-secretase transmembrane sequence in metal ion mediated oligomerization | |
Mathé et al. | Fe3+-Hydroxide Ligation in the Superoxide Reductase from Desulfoarculus b aarsii Is Associated with pH Dependent Spectral Changes | |
de Vitry et al. | Biochemical and spectroscopic characterization of the covalent binding of heme to cytochrome b 6 |