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Journal ArticleDOI

Magnetic circular dichroism studies of myoglobin complexes. Correlations with heme spin state and axial ligation.

Larry E. Vickery, +2 more
- 21 Jan 1976 - 
- Vol. 98, Iss: 2, pp 343-350
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This article is published in Journal of the American Chemical Society.The article was published on 1976-01-21. It has received 151 citations till now. The article focuses on the topics: Vibrational circular dichroism & Circular dichroism.

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Journal ArticleDOI

Spectroscopic investigations of ferric cytochrome P-450-CAM ligand complexes. Identification of the ligand trans to cysteinate in the native enzyme.

TL;DR: Close examination of all spectral data reveals that amino acid analog adducts of P-450-CAM with amides and, in particular, alcohols produce spectra that almost exactly duplicate those of native P- 450 and suggests that the ligand trans to cysteinate in the six-coordinate ferric enzyme has an oxygen donor atom.
Book ChapterDOI

Polarized absorption and linear dichroism spectroscopy of hemoglobin.

TL;DR: This chapter is concerned with polarized absorption and linear dichroism spectroscopy of hemoglobin, techniques used to study the optical properties of oriented systems.
Journal ArticleDOI

Artificial oxygen carriers, hemoglobin vesicles and albumin-hemes, based on bioconjugate chemistry.

TL;DR: Manipulation of physicochemical parameters of HbV, such as O(2) binding affinity and suspension rheology, supports the use of HBV for versatile medical applications.
Journal ArticleDOI

Coordination structure of the ferric heme iron in engineered distal histidine myoglobin mutants

TL;DR: Recombinant human myoglobin mutants with the distal His residue replaced by Leu, Val, or Gln residues were prepared by site-directed mutagenesis and expression in Escherichia coli to study the ligand binding properties.
Book ChapterDOI

Magnetic Circular Dichroism of Hemoproteins.

TL;DR: In this article, the authors describe the progress made over the last 10 years in studies of the magnetic circular dichroism (MCD) spectra of heme models and proteins.
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