Localization of Histidine Residues Responsible for Heme Axial Ligation in Cytochrome b556 of Complex II (Succinate:Ubiquinone Oxidoreductase) in Escherichia coli-Reference-Cited by-同舟云学术

Localization of Histidine Residues Responsible for Heme Axial Ligation in Cytochrome b556 of Complex II (Succinate:Ubiquinone Oxidoreductase) in Escherichia coli

Published:1998-03-01 Issue:12 Volume:37 Page:4148-4159
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Vibat Cecile Rose T.¹,Cecchini Gary¹,Nakamura Kayako¹,Kita Kiyoshi¹,Gennis Robert B.¹

Affiliation:

1. Department of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, Molecular Biology (151-S), Veterans Administration Medical Center, San Francisco, California, Department of Biochemistry and Biophysics, University of California, San Francisco, California, and Department of Parasitology, The Institute of Medical Science, Tokyo University, Japan

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi9716635

Reference62 articles.

1. Hederstedt, L., and Ohnishi, T. (1992) inMolecular Mechanisms in Bioenergetics(Ernster, L., Ed.) Vol. 23, pp 163−198, Elsevier Science Publishers, New York.

2. Nucleotide sequence encoding the flavoprotein and hydrophobic subunits of the succinate dehydrogenase of Escherichia coli

3. Nucleotide sequence encoding the iron-sulphur protein subunit of the succinate dehydrogenase of Escherichia coli

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