کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
5371469 1503955 2010 14 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Structure and reactivity of hexacoordinate hemoglobins
موضوعات مرتبط
مهندسی و علوم پایه شیمی شیمی تئوریک و عملی
پیش نمایش صفحه اول مقاله
Structure and reactivity of hexacoordinate hemoglobins
چکیده انگلیسی

The heme prosthetic group in hemoglobins is most often attached to the globin through coordination of either one or two histidine side chains. Those proteins with one histidine coordinating the heme iron are called “pentacoordinate” hemoglobins, a group represented by red blood cell hemoglobin and most other oxygen transporters. Those with two histidines are called “hexacoordinate hemoglobins”, which have broad representation among eukaryotes. Coordination of the second histidine in hexacoordinate Hbs is reversible, allowing for binding of exogenous ligands like oxygen, carbon monoxide, and nitric oxide. Research over the past several years has produced a fairly detailed picture of the structure and biochemistry of hexacoordinate hemoglobins from several species including neuroglobin and cytoglobin in animals, and the nonsymbiotic hemoglobins in plants. However, a clear understanding of the physiological functions of these proteins remains an elusive goal.

Graphical AbstractResearch Highlights►A review of hexacoordinate hemoglobin structure and function. ►The phylogeny of hexacoordinate hemoglobins. ►A review of ligand binding to hexacoordinate hemoglobins.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biophysical Chemistry - Volume 152, Issues 1–3, November 2010, Pages 1-14
نویسندگان
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