31P-NMR investigation of trimethylphosphine binding to [αFe(II),βMn(II)] hybrid hemoglobin
Author:
Publisher
Elsevier BV
Subject
Organic Chemistry,Biochemistry,Biophysics
Reference28 articles.
1. On the nature of allosteric transitions: A plausible model
2. Comparison of Experimental Binding Data and Theoretical Models in Proteins Containing Subunits*
3. Stereochemistry of Cooperative Effects in Haemoglobin: Haem–Haem Interaction and the Problem of Allostery
4. A mathematical model for structure-function relations in hemoglobin
5. The Three-State Model: A Minimal Allosteric Description of Homotropic and Heterotropic Effects in the Binding of Ligands to Hemoglobin
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1. Identity, Evolution, and Acidity of Partially Framework-Coordinated Al Species in Zeolites Probed by TMP 31P-NMR and FTIR;ACS Catalysis;2023-03-28
2. Effect of Copper State in Cu/H-ZSM-5 on Methane Activation by Brønsted Acid Sites, Studied by 1H MAS NMR In Situ Monitoring the H/D Hydrogen Exchange of the Alkane with Brønsted Acid Sites;The Journal of Physical Chemistry C;2021-01-18
3. Metal Ion Reconstituted Hybrid Hemoglobins;Progress in Inorganic Chemistry;2007-03-09
4. Effect of Phosphorus Axial π-Acceptors in Iron(III) Porphyrinates: Characterization of Low-Spin Complexes [(PPh(OMe)2)2Fe(T(p-Me)PP)]CF3SO3 and [(PPh(OEt)2)2Fe(T(p-Me)PP)]CF3SO3;Inorganic Chemistry;1997-12-01
5. Phosphines as structural and functional probes of hemoproteins;Coordination Chemistry Reviews;1997-10
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