A Serine → Cysteine Ligand Mutation in the High Potential Iron−Sulfur Protein from Chromatium vinosum Provides Insight into the Electronic Structure of the [4Fe−4S] Cluster-Reference-Cited by-同舟云学术

A Serine → Cysteine Ligand Mutation in the High Potential Iron−Sulfur Protein from Chromatium vinosum Provides Insight into the Electronic Structure of the [4Fe−4S] Cluster

Published:1996-01-01 Issue:1 Volume:118 Page:75-80
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Babini Elena¹,Bertini Ivano¹,Borsari Marco¹,Capozzi Francesco¹,Dikiy Alexander¹,Eltis Lindsay D.¹,Luchinat Claudio¹

Affiliation:

1. Contribution from the Institute of Agricultural Chemistry, University of Bologna, Viale Berti Pichat, 10 40127 Bologna, Italy, Department of Biochemistry, Université Laval, Québec City, Québec G1K 7P4, Canada, Department of Chemistry, University of Florence, Via Gino Capponi, 7, 50121 Florence, Italy, and Department of Chemistry, University of Modena, Via Campi 183, 41100 Modena, Italy

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja952636%2B

Reference40 articles.

1. Exchange coupling and resonance delocalization in reduced iron-sulfur [Fe4S4]+ and iron-selenium [Fe4Se4]+ clusters. 2. A generalized nonlinear model for spin-state energies and EPR and hyperfine properties

2. Sharp-line electronic spectroscopy and metal-ligand geometry in the pentaamminehydroxochromium(III) complex

3. A model for the spin states of high-potential iron-sulfur [Fe4S4]3+ proteins

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