Leghaemoglobin: a model for the investigation of haem protein axial ligation

Deborah K. Jones; Neesha Patel; Myles R. Cheesman; Andrew J. Thomson; Emma Lloyd Raven

doi:10.1016/S0020-1693(02)00689-8

Leghaemoglobin: a model for the investigation of haem protein axial ligation

Deborah K. Jones, Neesha Patel, Myles R. Cheesman, Andrew J. Thomson, Emma Lloyd Raven

Research output: Contribution to journal › Article › peer-review

4 Citations (Scopus)

Abstract

The structural identity of the axial ligands is one of the major determinants of haem protein function and properties. In this work, the mobile distal histidine residue of soybean leghaemoglobin a has been replaced with a non-coordinating alanine residue (H61A variant) and the H61A variant has been characterised using a range of spectroscopic methods. These experiments provide a useful experimental framework for the examination of haem axial ligation and structure- function relationships.

Original language	English
Pages (from-to)	303-309
Number of pages	7
Journal	Inorganica Chimica Acta
Volume	331
Issue number	1
DOIs	https://doi.org/10.1016/S0020-1693(02)00689-8
Publication status	Published - 2002

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10.1016/S0020-1693(02)00689-8

Cite this

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title = "Leghaemoglobin: a model for the investigation of haem protein axial ligation",

abstract = "The structural identity of the axial ligands is one of the major determinants of haem protein function and properties. In this work, the mobile distal histidine residue of soybean leghaemoglobin a has been replaced with a non-coordinating alanine residue (H61A variant) and the H61A variant has been characterised using a range of spectroscopic methods. These experiments provide a useful experimental framework for the examination of haem axial ligation and structure- function relationships.",

author = "Jones, {Deborah K.} and Neesha Patel and Cheesman, {Myles R.} and Thomson, {Andrew J.} and Raven, {Emma Lloyd}",

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AU - Patel, Neesha

AU - Cheesman, Myles R.

AU - Thomson, Andrew J.

AU - Raven, Emma Lloyd

PY - 2002

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AB - The structural identity of the axial ligands is one of the major determinants of haem protein function and properties. In this work, the mobile distal histidine residue of soybean leghaemoglobin a has been replaced with a non-coordinating alanine residue (H61A variant) and the H61A variant has been characterised using a range of spectroscopic methods. These experiments provide a useful experimental framework for the examination of haem axial ligation and structure- function relationships.

U2 - 10.1016/S0020-1693(02)00689-8

DO - 10.1016/S0020-1693(02)00689-8

M3 - Article

VL - 331

SP - 303

EP - 309

JO - Inorganica Chimica Acta

JF - Inorganica Chimica Acta

SN - 0020-1693

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