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Structural and electronic properties of the liver fluke hemoglobin heme cavity by nuclear magnetic resonance: hemin isotope labeling.

Abstract：

:Reconstitution of liver fluke (Dicrocoelium dendriticum) apo-hemoglobin with hemins selectively deuterated at specific positions has permitted the assignment of several heme resonances in the proton nuclear magnetic resonance spectrum of the Met-aquo and Met-cyano forms of the holoprotein. It was established that in the Met-aquo form the meso protons resonate at positions characteristic of a six-co-ordinated in-plane iron. From this, we deduced that the Met-aquo species retains a bound water molecule at pH values as low as 4.5. The orientation of the proximal histidine imidazole ring with respect to the heme group in the cavity was determined through the identification of the heme methyl signals and the analysis of the hyperfine shift pattern in the Met-cyano hemoglobin proton nuclear magnetic resonance spectrum. Compared to sperm whale myoglobin, the heme appears to be rotated by 180 degrees about the alpha, gamma meso-axis. Protein isomers with the heme group in a reversed orientation were not detected, even shortly after reconstitution. In the Met-cyano form, the resonances most affected by the Bohr transition were shown to arise from the heme propionates.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Lecomte JT,La Mar GN,Smit JD,Winterhalter KH,Smith KM,Langry KC,Leung HK

doi

10.1016/0022-2836(87)90612-7

subject

Has Abstract

pub_date

1987-09-05 00:00:00

pages

101-10

issue

1

eissn

0022-2836

issn

1089-8638

pii

0022-2836(87)90612-7

journal_volume

197

pub_type

杂志文章

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