O2 and Water Migration Pathways between the Solvent and Heme Pockets of Hemoglobin with Open and Closed Conformations of the Distal HisE7-Reference-Cited by-同舟云学术

O2 and Water Migration Pathways between the Solvent and Heme Pockets of Hemoglobin with Open and Closed Conformations of the Distal HisE7

Published:2015-08-19 Issue:34 Volume:54 Page:5279-5289
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Shadrina Maria S.¹,Peslherbe Gilles H.¹,English Ann M.¹

Affiliation:

1. Department of Chemistry and Biochemistry, Centre for Research in Molecular Modeling and PROTEO, Concordia University, Montreal, Quebec H4B 1R6, Canada

Funder

Government of Canada

Concordia University

Fonds de Recherche du Qu??bec - Nature et Technologies

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.5b00369

Reference44 articles.

1. NMR reveals hydrogen bonds between oxygen and distal histidines in oxyhemoglobin

2. Distal Histidine Stabilizes Bound O2 and Acts as a Gate for Ligand Entry in Both Subunits of Adult Human Hemoglobin

3. An X-ray study of azide methaemoglobin

4. Investigations of Ligand Association and Dissociation Rates in the "Open" and "Closed" States of Myoglobin

5. Conformational interconversion in protein crystals

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