Influence of allosteric effectors on the heme conformation of dromedary ferrous nitrosylhemoglobin detected by XANES spectroscopy. 1991

A Congiu Castellano, and S Della Longa, and A Bianconi, and M Barteri, and E Burattini, and P Ascenzi, and M Coletta, and R Santucci, and G Amiconi
Department of Physics, University of Roma, La Sapienza, Italy.

The changes of the Fe heme-active site conformation of dromedary (Camelus dromedarius) nitrosylhemoglobin (HbNO) induced by inositol hexakisphosphate (IHP) and chlofibric acid (CFA) have been studied by using X-ray absorption near-edge structure (XANES) spectroscopy. Structural information has been determined by multiple scattering analysis of the Fe K-edge XANES spectra. The proximal histidine is found to move away from iron centers by about 0.4 Angstrom on the average over the four hemes upon binding of CFA or stoichiometric amount of IHP. In molar excess of polyanion or in the simultaneous presence of IHP, CFA and chloride, the proximal histidine moves back to a position very close to that observed in pure buffer; yet, the structure modulation induced by the allosteric effectors is not completely reversible. Such findings parallel with the functional properties and the spectroscopic (e.g., EPR and absorbance) characteristics of HbNO.

UI MeSH Term Description Entries
D008024 Ligands A molecule that binds to another molecule, used especially to refer to a small molecule that binds specifically to a larger molecule, e.g., an antigen binding to an antibody, a hormone or neurotransmitter binding to a receptor, or a substrate or allosteric effector binding to an enzyme. Ligands are also molecules that donate or accept a pair of electrons to form a coordinate covalent bond with the central metal atom of a coordination complex. (From Dorland, 27th ed) Ligand
D008968 Molecular Conformation The characteristic three-dimensional shape of a molecule. Molecular Configuration,3D Molecular Structure,Configuration, Molecular,Molecular Structure, Three Dimensional,Three Dimensional Molecular Structure,3D Molecular Structures,Configurations, Molecular,Conformation, Molecular,Conformations, Molecular,Molecular Configurations,Molecular Conformations,Molecular Structure, 3D,Molecular Structures, 3D,Structure, 3D Molecular,Structures, 3D Molecular
D010833 Phytic Acid Complexing agent for removal of traces of heavy metal ions. It acts also as a hypocalcemic agent. Inositol Hexaphosphate,Phytin,Calcium Phytate,Inositol Hexakisphosphate,Phytate,Sodium Phytate,Acid, Phytic,Hexakisphosphate, Inositol,Hexaphosphate, Inositol,Phytate, Calcium,Phytate, Sodium
D002162 Camelus Two-toed, hoofed mammals with four legs, a big-lipped snout, and a humped back belonging to the family Camelidae. They are native to North Africa, and Western and Central Asia. Camels,Dromedary,Bactrian Camels,Bractrian Camels,Camelus bactrianus,Camelus dromedarius,Bactrian Camel,Bractrian Camel,Camel,Camel, Bactrian,Camel, Bractrian,Camels, Bactrian,Camels, Bractrian,Dromedaries
D002994 Clofibrate A fibric acid derivative used in the treatment of HYPERLIPOPROTEINEMIA TYPE III and severe HYPERTRIGLYCERIDEMIA. (From Martindale, The Extra Pharmacopoeia, 30th ed, p986) Athromidin,Atromid,Atromid S,Clofibric Acid, Ethyl Ester,Ethyl Chlorophenoxyisobutyrate,Miscleron,Miskleron,Chlorophenoxyisobutyrate, Ethyl
D006418 Heme The color-furnishing portion of hemoglobin. It is found free in tissues and as the prosthetic group in many hemeproteins. Ferroprotoporphyrin,Protoheme,Haem,Heme b,Protoheme IX
D006454 Hemoglobins The oxygen-carrying proteins of ERYTHROCYTES. They are found in all vertebrates and some invertebrates. The number of globin subunits in the hemoglobin quaternary structure differs between species. Structures range from monomeric to a variety of multimeric arrangements. Eryhem,Ferrous Hemoglobin,Hemoglobin,Hemoglobin, Ferrous
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D001665 Binding Sites The parts of a macromolecule that directly participate in its specific combination with another molecule. Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D013057 Spectrum Analysis The measurement of the amplitude of the components of a complex waveform throughout the frequency range of the waveform. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed) Spectroscopy,Analysis, Spectrum,Spectrometry

Related Publications

A Congiu Castellano, and S Della Longa, and A Bianconi, and M Barteri, and E Burattini, and P Ascenzi, and M Coletta, and R Santucci, and G Amiconi
April 2005, The European physical journal. E, Soft matter,
A Congiu Castellano, and S Della Longa, and A Bianconi, and M Barteri, and E Burattini, and P Ascenzi, and M Coletta, and R Santucci, and G Amiconi
January 1974, Acta biologica et medica Germanica,
A Congiu Castellano, and S Della Longa, and A Bianconi, and M Barteri, and E Burattini, and P Ascenzi, and M Coletta, and R Santucci, and G Amiconi
October 2018, Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry,
A Congiu Castellano, and S Della Longa, and A Bianconi, and M Barteri, and E Burattini, and P Ascenzi, and M Coletta, and R Santucci, and G Amiconi
January 1970, Acta biochimica et biophysica; Academiae Scientiarum Hungaricae,
A Congiu Castellano, and S Della Longa, and A Bianconi, and M Barteri, and E Burattini, and P Ascenzi, and M Coletta, and R Santucci, and G Amiconi
December 1991, Biochimica et biophysica acta,
A Congiu Castellano, and S Della Longa, and A Bianconi, and M Barteri, and E Burattini, and P Ascenzi, and M Coletta, and R Santucci, and G Amiconi
July 1972, FEBS letters,
A Congiu Castellano, and S Della Longa, and A Bianconi, and M Barteri, and E Burattini, and P Ascenzi, and M Coletta, and R Santucci, and G Amiconi
January 1976, Biochemistry,
A Congiu Castellano, and S Della Longa, and A Bianconi, and M Barteri, and E Burattini, and P Ascenzi, and M Coletta, and R Santucci, and G Amiconi
January 1972, Journal of biochemistry,
A Congiu Castellano, and S Della Longa, and A Bianconi, and M Barteri, and E Burattini, and P Ascenzi, and M Coletta, and R Santucci, and G Amiconi
February 1986, The Journal of biological chemistry,
A Congiu Castellano, and S Della Longa, and A Bianconi, and M Barteri, and E Burattini, and P Ascenzi, and M Coletta, and R Santucci, and G Amiconi
September 1980, The Biochemical journal,
Copied contents to your clipboard!