First observation by mass spectrometry of a 3+ oxidation state for a [4Fe-4S] metalloprotein: An ESI-FTICR mass spectrometry study of the high potential iron-sulfur protein from Chromatium vinosum-Reference-Cited by-同舟云学术

First observation by mass spectrometry of a 3+ oxidation state for a [4Fe-4S] metalloprotein: An ESI-FTICR mass spectrometry study of the high potential iron-sulfur protein from Chromatium vinosum

Published:2001-07-01 Issue:7 Volume:12 Page:819-825
ISSN:1044-0305
Container-title:Journal of the American Society for Mass Spectrometry
language:en
Short-container-title:J. Am. Soc. Mass Spectrom.

Author:

Johnson Keith A.¹,Amster I. Jonathan¹

Affiliation:

1. Department of Chemistry, The University of Georgia, Athens, Georgia, USA

Publisher

American Chemical Society (ACS)

Subject

Spectroscopy,Structural Biology

Link

https://pubs.acs.org/doi/pdf/10.1016/S1044-0305%2801%2900263-X

Reference34 articles.

1. Johnson, M. K.King, R. B. Iron-Sulfur Clusters1994ChichesterWiley18961915

2. Probing the Stoichiometry and Oxidation States of Metal Centers in Iron−Sulfur Proteins Using Electrospray FTICR Mass Spectrometry

3. Zinc-induced conformational changes in the DNA-binding domain of the vitamin D receptor determined by electrospray ionization mass spectrometry

4. Zinc-Induced Conformational Transitions of Acidic Peptides: Characterization by Circular Dichroism and Electrospray Mass Spectrometry

5. Preparation and Characterization of [2Ga-2S] Anabaena 7120 Ferredoxin, the First Gallium−Sulfur Cluster-Containing Protein

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