Hydrogen-1 nuclear magnetic resonance investigation of high-potential iron-sulfur proteins from Ectothiorhodospira halophila and Ectothiorhodospira vacuolata: a comparative study of hyperfine-shifted resonances-Reference-Cited by-同舟云学术

Hydrogen-1 nuclear magnetic resonance investigation of high-potential iron-sulfur proteins from Ectothiorhodospira halophila and Ectothiorhodospira vacuolata: a comparative study of hyperfine-shifted resonances

Published:1986-01-14 Issue:1 Volume:25 Page:60-67
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Krishnamoorthi R.,Markley John L.,Cusanovich Michael A.,Przysiecki C. T.,Meyer T. E.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00349a010

Reference30 articles.

1. NH---S hydrogen bonds in Peptococcus aerogenes ferredoxin, Clostridium pasteurianum rubredoxin, and Chromatium high potential iron protein.

2. [35] Purification of (4Fe-4S)1—2− ferrodoxins (high-potential iron-sulfur proteins) from bacteria

3. Carter, C. W., Jr. (1977a) in Iron-Sulfur Proteins(Lovenberg, W., Ed.) Vol. Ill, pp157-204, Academic Press, New York.

4. New stereochemical analogies between iron-sulfur electron transport proteins.

5. Comparison of Oxidation-Reduction Site Geometries in Oxidized and Reduced Chromatium High Potential Iron Protein and Oxidized Peptococcus aerogenes Ferredoxin

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