Results 121 to 130 of about 1,955 (147)
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Spin and electron distributions in heme-cyanide models and hemeproteins

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1985
Proton NMR spectra of low-spin Fe(III) cyanoprotoheme as prosthetic group in a number of proteins are presented. The diagonally positioned 1-, 5- and 3-, 8-methyl groups obey shifts proportional to the Fe(III)/(II) reduction potential Em7, which indicates a pseudo-contact interaction.
J, Paul   +3 more
openaire   +2 more sources

Azanone (HNO) interaction with Hemeproteins and metalloporphyrins

2012
Abstract Azanone (HNO), also called nitroxyl, is a highly reactive compound, with interesting yet poorly understood biological properties. Like its closely related sibling NO, its main biological targets are heme proteins, although significant differences in their reactivity and pharmacological effects are observed.
Doctorovich, Fabio   +4 more
openaire   +2 more sources

Optical rotatory dispersion of a respiratory hemeprotein of Chrinomus thummi

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1968
Abstract The spatial structure of an O 2 -binding hemeprotein obtained from Chironomus thummi is compared with that of sperm whale myoglobin by means of rotatory dispersion. The optical rotation at the 233-mμ minimum of the ultraviolet Cotton effect is only 70% of the value obtained for myoglobin.
H, Formanek, J, Engel
openaire   +2 more sources

Protein Fluctuations and Hemeprotein Affinity for Ligand

1986
Binding processes in hemeproteins involve the iron atom and the protein properties: structural and dynamics. Crystallographic data of Perutz have given an appreciate popularity to a correlation between the displacement of the iron out of the porphyrin plane and the affinity of the hemeprotein for ligand.
openaire   +1 more source

Vibrational Circular Dichroism of Ligand Vibrations in Hemeprotein

1995
The distal amino acid residues in myoglobin (Mb) and hemoglobin (Hb) are elaborately designed to control the chemical reactions of ligands to the heme iron. Many techniques have been applied to elucidate the reaction mechanism of ligand binding in heme pockets.
J. Teraoka   +4 more
openaire   +1 more source

Hemes and hemeproteins

Journal of Inorganic Biochemistry, 1986
David A. Baldwin   +2 more
openaire   +1 more source

PI‐INTERACTIONS IN METALLOPORPHYRINS AND HEMEPROTEINS*

Annals of the New York Academy of Sciences, 1969
W S, Caughey   +4 more
openaire   +2 more sources

CARBON MONOXIDE BONDING IN HEMEPROTEINS *

Annals of the New York Academy of Sciences, 1970
openaire   +2 more sources

Circular dichroism studies of acid⇌alkaline transition on hemeproteins

Journal of Chemical Sciences, 1993
D V Behere, Sandeep Modi
exaly  

Global substitution of hemeproteins with noncanonical amino acids in with intact cofactor maturation machinery

Enzyme and Microbial Technology, 2017
Nediljko Budisa   +2 more
exaly  

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