Comparison of heme environments and proximal ligands in peroxidases and other hemoproteins through carbon-13 nuclear magnetic resonance spectroscopy of carbon monoxide complexes-Reference-Cited by-同舟云学术

Comparison of heme environments and proximal ligands in peroxidases and other hemoproteins through carbon-13 nuclear magnetic resonance spectroscopy of carbon monoxide complexes

Published:1985-09 Issue:2 Volume:131 Page:607-613
ISSN:0006-291X
Container-title:Biochemical and Biophysical Research Communications
language:en
Short-container-title:Biochemical and Biophysical Research Communications

Author:

Behere D.V.,Gonzalez-Vergara Enrlque,Goff Harold M.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference29 articles.

1. Methods for Determining Metal Ion Envionments in Proteins: Structure and Function of Metalloproteins;Caughey,1980

2. Crystallization-induced changes in protein structure observed by infrared spectroscopy of carbon monoxide liganded to human hemoglobins A and Zurich

3. Natural abundance 13 C spectra of proteins: Carboxy-myoglobin and hemoglobin

4. Nuclear magnetic resonance studies of carbon-13 monoxide binding to various hemoglobins

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