Simulation of the electron-paramagnetic-resonance spectrum of the iron-protein of nitrogenase. A prediction of the existence of a second paramagnetic centre.

The Biochemical journal ·Vol. 175 ·No. 3 ·1978-12-01 ·Pages 955-7

Lowe DJ

Abstract

The e.p.r. spectra of the Fe-proteins of nitrogenase from all sources studied have unusual features in that they have very anisotropic linewidths and low integrated intensities. These characteristics can be explained by assuming that one of the two electrons accepted by these proteins is located at a rapidly relaxing paramagnetic centre that is unobservable by e.p.r., but causes anisotropic broadening of the e.p.r. signal of the other electron. Complex-formation between Fe-proteins and MgATP is described in terms of a 50-60 degrees rotation of the e.p.r.-observable centre.

MeSH Terms

Chemical Phenomena Chemistry Electron Spin Resonance Spectroscopy Iron Metalloproteins/analysis Models, Chemical Nitrogenase

Chemicals

Metalloproteins Iron Nitrogenase

Authors & Affiliations

1 authors, click to expand affiliations / ORCID

Lowe D J

References (12)

12 references, click to expand

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Article Info

Journal

The Biochemical journal

Abbr.

Biochem J

ISSN

0264-6021

DOI

10.1042/bj1750955

Published

1978-12-01

Pages

955-7

Language

English

Region

England

NLM ID

2984726R

PMCID

PMC1186158

Subset

External Links

PubMed source DOI: 10.1042/bj1750955 PMC Full Text View journal details

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Simulation of the electron-paramagnetic-resonance spectrum of the iron-protein of nitrogenase. A prediction of the existence of a second paramagnetic centre.

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