Distinct domain responses of R-state human hemoglobins A, C, and S to anions.

No abstract is available for this paper.

• Publication year

  2002

• Venue

  Blood Cells, Molecules & Diseases

• Publication date

  2002-07-01

• Fields of study

  Medicine, Chemistry

• Identifiers
  DOI 10.1006/BCMD.2002.0546PMID 12482413
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Heme Redox Properties of S-Nitrosated Hemoglobin A0 and Hemoglobin S

  2002cited by this paper
• Heme-Protein Fluorescence

  2002cited by this paper
• Concentration-dependent Effects of Anions on the Anaerobic Oxidation of Hemoglobin and Myoglobin*

  2000cited by this paper
• Reaction of hydrogen peroxide with ferrylhemoglobin: superoxide production and heme degradation.

  2000cited by this paper
• Cysteines beta93 and beta112 as probes of conformational and functional events at the human hemoglobin subunit interfaces.

  1999cited by this paper
• Solution-active structural alterations in liganded hemoglobins C (beta6 Glu --> Lys) and S (beta6 Glu --> Val).

  1999cited by this paper
• Cysteines β93 and β112 as Probes of Conformational and Functional Events at the Human Hemoglobin Subunit Interfaces

  1999cited by this paper
• Solution-active Structural Alterations in Liganded Hemoglobins C (β6 Glu → Lys) and S (β6 Glu → Val)*

  1999cited by this paper
• Conformational Differences in CO Derivatives of HbA, HbC (Eβ6K) and HbS (Eβ6V) in the Presence and Absence of Inositol Hexaphosphate Detected Using Ultraviolet Resonance Raman Spectroscopy

  1998cited by this paper
• Comparative oxidation of hemoglobins A and S.

  1998cited by this paper
• Formation of fluorescent heme degradation products during the oxidation of hemoglobin by hydrogen peroxide.

  1998cited by this paper
• Energetic components of the allosteric machinery in hemoglobin measured by hydrogen exchange.

  1998cited by this paper
• Conformational fluctuations in deoxy hemoglobin revealed as a major contributor to anionic modulation of function through studies of the oxygenation and oxidation of hemoglobins A0 and Deer Lodge beta2(NA2)His --> Arg.

  1998cited by this paper
• Alteration of redox stability of hemoglobins A and S by biological buffers.

  1998cited by this paper
• Probing the Hemoglobin Central Cavity by Direct Quantification of Effector Binding Using Fluorescence Lifetime Methods*

  1997cited by this paper
• Blood flow regulation by S-nitrosohemoglobin in the physiological oxygen gradient.

  1997cited by this paper
• Conformational Changes in Oxyhemoglobin C (Glu Lys) Detected by Spectroscopic Probing (*)

  1996cited by this paper
• S-nitrosohaemoglobin: a dynamic activity of blood involved in vascular control

  1996cited by this paper
• A Spectroelectrochemical Method for Differentiation of Steric and Electronic Effects in Hemoglobins and Myoglobins (*)

  1995cited by this paper
• Reaction of human hemoglobin HbA0 and two cross-linked derivatives with hydrogen peroxide: differential behavior of the ferryl intermediate.

  1995cited by this paper
• The chloride effect in human haemoglobin. A new kind of allosteric mechanism.

  1994cited by this paper
• Front-face fluorescence spectroscopy of hemoglobins.

  1994cited by this paper
• Chloride masks effects of opposing positive charges in Hb A and Hb Hinsdale (beta 139 Asn-->Lys) that can modulate cooperativity as well as oxygen affinity.

  1994cited by this paper
• Random chemical modification of the oxygen-linked chloride-binding sites of hemoglobin: Those in the central dyad axis may influence the transition between deoxy- and oxy-hemoglobin

  1993cited by this paper
• The functional, oxygen-linked chloride binding sites of hemoglobin are contiguous within a channel in the central cavity

  1992cited by this paper
• The sickle erythrocyte in double jeopardy: autoxidation and iron decompartmentalization.

  1990cited by this paper
• Oxidative reactions of hemoglobin.

  1990cited by this paper
• [26] Oxidative reactions of hemoglobin

  1990cited by this paper
• Steady-state fluorescence emission from the fluorescent probe, 5-iodoacetamidofluorescein, bound to hemoglobin.

  1986cited by this paper
• Distal and proximal control of ligand reactivity: a transient Raman comparison of COHbA and COHb (Zurich)

  1985cited by this paper
• Subunit heterogeneity in the structure and dynamics of hemoglobin

  1983cited by this paper
• The detection of hemoglobin dimers by intrinsic fluorescence.

  1983cited by this paper
• Allosteric Effects in Haemoglobin

  1982cited by this paper
• Mechanism of autooxidation for hemoglobins and myoglobins. Promotion of superoxide production by protons and anions.

  1982cited by this paper
• Tryptophan fluorescence of human hemoglobin. I. Significant change of fluorescence intensity and lifetimes in the T - R transition.

  1981cited by this paper
• Intrinsic fluorescence emission of intact oxy hemoglobins.

  1980cited by this paper
• Identification of chloride-binding sites in hemoglobin by nuclear-magnetic-resonance quadrupole-relaxation studies of hemoglobin digests.

  1975cited by this paper
• The effect of potassium chloride on the Bohr effect of human hemoglobin.

  1975cited by this paper
• Observations on the mechanical precipitation of oxy Hb S and other mutants.

  1975cited by this paper
• Mechanical stability of hemoglobin subunits: an abnormality in betaS-subunits of sickle hemoglobin.

  1974cited by this paper
• A role for chloride in the autoxidation of hemoglobin under conditions similar to those in erythrocytes

  1974cited by this paper
• Ligand binding and release of an analogue of 2,3-diphosphoglycerate from human hemoglobin.

  1972cited by this paper
• Nuclear magnetic resonance quadrupole relaxation studies of chloride binding to human oxy- and deoxyhaemoglobin.

  1972cited by this paper
• Enzyme Proteins. (Book Reviews: Hemoglobin and Myoglobin in Their Reactions with Ligands)

  1971cited by this paper
• Use of a fluorescent analogue of 2,3-diphosphoglycerate as a probe of human hemoglobin conformation during carbon monoxide binding.

  1971cited by this paper
• SULFHYDRYL GROUPS AND THE STRUCTURE OF HEMOGLOBIN

  1956cited by this paper

• Central role for NMDA receptors in redox mediated impairment of synaptic function during aging and Alzheimer's disease

  2017cites this paper
• Phase separation and crystallization of hemoglobin C in transgenic mouse and human erythrocytes.

  2008cites this paper
• Oxidative Reactions of Normal and Abnormal Hemoglobins in the Presence of Phosphatidylserine Vesicles

  2005cites this paper
• Liganded hemoglobin structural perturbations by the allosteric effector L35.

  2005cites this paper
• Oxidative reactions of normal and abnormal hemoglobins in the presence of phosphatidylserine vesicles.

  2005cites this paper
• Oxidative reactions of normal and abnormal hemoglobins in the presence of phosphatidylserine vesicles.

  2005cites this paper
• Quantification of Effector Binding to the Hemoglobin Central Cavity by Intrinsic and Extrinsic Steady-State Fluorescence

  2004cites this paper
• Generation of transgenic mice expressing human hemoglobin E.

  2004cites this paper