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2. Proton magnetic resonance study of the histidine residues of horse myoglobin

Author

Thompson, John C., Haar, Wolfgang, Maurer, Wolfgang, Rüterjans, Heinrich, Gersonde, Klaus, Sick, Hinrich, and Publica

Subjects
chemistry.chemical_classification, biology, Chemistry, Stereochemistry, Biophysics, chemistry.chemical_element, Cell Biology, Biochemistry, Oxygen, chemistry.chemical_compound, Enzyme, Monomer, Protein structure, Myoglobin, Structural Biology, Genetics, biology.protein, Titration, Ribonuclease, Molecular Biology, Histidine
Abstract

In recent years proton magnetic resonance methods have proven useful in the study of protein structure, particularly in the investigations of histidine residues which have led to conclusions about the active sites of the enzymes ribonuclease A [l-3] and ribonuclease Tr [4,5]. In this communication we report the results of a proton magnetic resonance investigation in ‘H,O of the histidine residues of horse myoglobin with the heme iron in the reduced state. Myoglobin, a monomeric oxygen transporting protein in mammalian muscle, has been widely studied and has been characterized structurally by X-ray diffraction studies [6-81 . Proton magnetic resonance studies [9-121 have been made przviously on myoglobin, but the titration behaviors of the histidine residues of reduced myoglobin have not before been reported. The results of an NMR-monitored, acid-base titration of horse CO-Mb (II)* reported here show that at least 6 histidine residues have ‘pp values** between 6.7 and 7.2.

Published
1971

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