The Unique Heme–Heme Interactions of the HomodimericScapharca inaequivalvisHemoglobin as Probed in the Protein Reconstituted with Unnatural 2,4 Heme Derivatives-Reference-Cited by-同舟云学术

The Unique Heme–Heme Interactions of the HomodimericScapharca inaequivalvisHemoglobin as Probed in the Protein Reconstituted with Unnatural 2,4 Heme Derivatives

Published:1997-03 Issue:2 Volume:339 Page:275-282
ISSN:0003-9861
Container-title:Archives of Biochemistry and Biophysics
language:en
Short-container-title:Archives of Biochemistry and Biophysics

Author:

Zamparelli Carlotta,Verzili Daniela,Boffi Alberto,Chiancone Emilia,Takahashi Satoshi,Rousseau Denis L.,Regan Rebecca,Gibson Quentin H.

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics

Reference24 articles.

1. Structural Transitions Upon Ligand Binding in a Cooperative Dimeric Hemoglobin

2. High-Resolution Crystallographic Analysis of a Co-operative Dimeric Hemoglobin

3. Regulation of Oxygen Affinity of Hemoglobin: Influence of Structure of the Globin on the Heme Iron

4. Kinetics of ligand binding and quaternary conformational change in the homodimeric hemoglobin from Scapharca inaequivalvis.

5. Ligand binding to the dimeric hemoglobin from Scapharca inaequivalvis, a hemoglobin with a novel mechanism for cooperativity

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