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Replacement of the methionine axial ligand in cytochrome c(550) by a lysine: effects on the haem electronic structure

Replacement of the methionine axial ligand in cytochrome c(550) by a lysine: effects on the haem electronic structure
Replacement of the methionine axial ligand in cytochrome c(550) by a lysine: effects on the haem electronic structure
The prosthetic group of low-spin haem proteins is an iron porphyrin with two axial ligands, typically histidine, methionine or lysine. Determining the geometry of the axial ligands is an important step in structural characterisation, particularly in the paramagnetic oxidised forms. This work extends earlier studies of the hyperfine nuclear magnetic resonance (NMR) shifts of haem substituents in bis-His and His-Met cytochromes to His-Lys co-ordination in the MINK mutant of Paracoccus versutus cytochrome c(550). The electronic structure of the His-Lys haem is shown to be similar to that produced by His-cyanide co-ordination, such that NMR can be used to determine the geometry of the His ligand.
paramagnetic nuclear magnetic resonance, cytochrome c, solution structure, site-specific mutagenesis, axial ligand, thiobacillus-versutus, heme ligation, shifts, nmr, paracoccus, proteins, c-13, orientation, met
0014-5793
185-188
Louro, Ricardo O.
8014cf88-eb58-4ecd-8e04-8ce90a4e43f6
de Waal, Ellen C.
8b504216-3e7c-460a-bbea-08399aa077a9
Ubbink, Marcellus
f770c556-0194-41f1-9f8a-d22c66bee1ab
Turner, David L.
6c4c1ccb-a6f2-47cf-944e-e69269198a29
Louro, Ricardo O.
8014cf88-eb58-4ecd-8e04-8ce90a4e43f6
de Waal, Ellen C.
8b504216-3e7c-460a-bbea-08399aa077a9
Ubbink, Marcellus
f770c556-0194-41f1-9f8a-d22c66bee1ab
Turner, David L.
6c4c1ccb-a6f2-47cf-944e-e69269198a29

Louro, Ricardo O., de Waal, Ellen C., Ubbink, Marcellus and Turner, David L. (2002) Replacement of the methionine axial ligand in cytochrome c(550) by a lysine: effects on the haem electronic structure. FEBS Letters, 510 (3), 185-188. (doi:10.1016/S0014-5793(01)03272-0).

Record type: Article

Abstract

The prosthetic group of low-spin haem proteins is an iron porphyrin with two axial ligands, typically histidine, methionine or lysine. Determining the geometry of the axial ligands is an important step in structural characterisation, particularly in the paramagnetic oxidised forms. This work extends earlier studies of the hyperfine nuclear magnetic resonance (NMR) shifts of haem substituents in bis-His and His-Met cytochromes to His-Lys co-ordination in the MINK mutant of Paracoccus versutus cytochrome c(550). The electronic structure of the His-Lys haem is shown to be similar to that produced by His-cyanide co-ordination, such that NMR can be used to determine the geometry of the His ligand.

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More information

Published date: 16 January 2002
Keywords: paramagnetic nuclear magnetic resonance, cytochrome c, solution structure, site-specific mutagenesis, axial ligand, thiobacillus-versutus, heme ligation, shifts, nmr, paracoccus, proteins, c-13, orientation, met

Identifiers

Local EPrints ID: 19808
URI: http://eprints.soton.ac.uk/id/eprint/19808
ISSN: 0014-5793
PURE UUID: 9250c445-7e46-47df-b5f4-93564b7c2c43

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Date deposited: 21 Feb 2006
Last modified: 08 Jan 2022 09:51

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Contributors

Author: Ricardo O. Louro
Author: Ellen C. de Waal
Author: Marcellus Ubbink
Author: David L. Turner

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