Parkhurst et al., 1970 - Google Patents
Kinetics of the reaction of hybrid-heme hemoglobins with carbon monoxideParkhurst et al., 1970
View PDF- Document ID
- 11441517891788164766
- Author
- Parkhurst L
- Geraci G
- Gibson Q
- Publication year
- Publication venue
- Journal of Biological Chemistry
External Links
Snippet
Hybrid-heme hemoglobins in which one chain contains meso-or deuteroheme and the other chain protoheme, react with CO at a slow rate characteristic of reduced hemoglobin rather than quickly reacting hemoglobin, but at a rate at the protoheme site that is somewhat faster …
- 108010054147 Hemoglobins 0 title abstract description 42
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| Traylor | Synthetic model compounds for hemoproteins | |
| Isied et al. | Electron transfer across polypeptides. 4. Intramolecular electron transfer from ruthenium (II) to iron (III) in histidine-33-modified horse heart cytochrome c | |
| Gibson | The contribution of the α and β chains to the kinetics of oxygen binding to and dissociation from hemoglobin | |
| Gray et al. | The effect of inositol hexaphosphate on the kinetics of CO and O2 binding by human hemoglobin | |
| Brinigar et al. | Solvent effects on reversible formation and oxidative stability of heme-oxygen complexes | |
| Mansouri et al. | Nonequivalence of chains in hemoglobin oxidation | |
| Antonini et al. | Studies on the Relations between Molecular and Functional Properties of Hemoglobin: VI. OBSERVATIONS ON THE KINETICS OF HEMOGLOBIN REACTIONS IN CONCENTRATED SALT SOLUTIONS | |
| Chang et al. | Carbon monoxide binding to pentacoordinate mercaptide-heme complexes: kinetic study on models for cytochrome P-450. | |
| Parkhurst et al. | Kinetics of the reaction of hybrid-heme hemoglobins with carbon monoxide | |
| Janick et al. | Characterization of complexes between Escherichia coli sulfite reductase hemoprotein subunit and its substrates sulfite and nitrite | |
| Dagdigian et al. | A new series of imidazole thioether chelating ligands for bioinorganic copper | |
| Wilting et al. | Conformational changes and ligand dissociation kinetics following rapid reduction of human aquomethemoglobin and horse aquometmyoglobin by hydrated electrons | |
| Azizi et al. | Rates of nitric oxide dissociation from hemoglobin | |
| Chiancone et al. | Kinetics of the reaction of the" masked" and" free" sulfhydryl groups of human hemoglobin with p-mercuribenzoate | |
| Goldbeck et al. | Magnetic circular dichroism study of cytochrome ba3 from Thermus thermophilus: spectral contributions from cytochromes b and a3 and nanosecond spectroscopy of carbon monoxide photodissociation intermediates | |
| Hill et al. | Low-spin ferric forms of cytochrome a 3 in mixed-ligand and partially reduced cyanide-bound derivatives of cytochrome c oxidase | |
| Aojula et al. | Functional consequences of haem orientational disorder in sperm-whale and yellow-fin-tuna myoglobins | |
| Satterlee et al. | Spectroscopic studies of the nature of ligand bonding in carbonmonoxyhemoglobins: evidence of a specific function for histidine-E7 from infrared and nuclear magnetic resonance intensities | |
| Kita et al. | Synthesis and optical resolution of (RhIII (S) 3 (N) 3) type complexes containing a thiolato, sulfenato, or sulfinato donor group. | |
| PRZYWARSKA‐BONIECKA et al. | Complexes of metal phthalocyanines with globin as the models of heme proteins | |
| Rubinow et al. | Cytochromes c'in their reaction with ethyl isocyanide | |
| Giacometti et al. | Binding of Carbon Monoxide to Hemoglobin Zürich: Proposal for a Kinetic Model | |
| Cassoly et al. | Structure and Function of Human Semihemoglobins α and β | |
| Darensbourg | Relative importance of. sigma. and. pi. bonding of molecular nitrogen and carbonyl in osmium (II) complexes as determined by infrared intensities of the molecular nitrogen and carbonyl stretching vibrations | |
| Kelley et al. | Kinetics and mechanism of the reactions between alkyl radicals and complexes of cobalt (III) and ruthenium (III) |