Abstract
Myoglobin is a small globular heme protein that increases the aerobic capacity of striated vertebrate muscle cells by taking up oxygen from blood during rest and delivering O2 to mitochondria during muscle contraction when blood flow through capillaries is restricted. The ferrous form of myoglobin can also react with CO and NO, which are produced in vivo as second messengers for regulating various physiological functions including blood pressure, platelet aggregation, and neurotransmission. Its tertiary structure consists of eight tightly packed helices, and the resulting “myoglobin fold” is very similar to that found for the α and β subunits of hemoglobin.
Highlights
From the Department of Biochemistry and Cell Biology and the W
This review focuses on NO, O2, and CO binding to myoglobin mutants under physiological conditions
Our current view is that the B states represent a number of ligand positions in the distal pocket with differing rates of approach to the iron atom
Summary
Vent is a much slower bimolecular process, which is not seen on the picosecond or nanosecond time scales shown in Fig. 2, and its rate is proportional to the total ligand concentration in the solution. Vent is a much slower bimolecular process, which is not seen on the picosecond or nanosecond time scales shown, and its rate is proportional to the total ligand concentration in the solution. These kinetic phenomena are most often interpreted in terms of the following consecutive reaction scheme. Jr. From the Department of Biochemistry and Cell Biology and the W. M. Keck Center for Computational Biology, Rice University, Houston, Texas 77005-1892. A or MbX aB1, · · ·, Bna ͓C1, · · ·, Cna X ϩ Mb ground state contact pair distal pocket?͒ free ligand (ps)
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