Heterologous Overexpression and Purification of Cytochrome c‘ from Rhodobacter capsulatus and a Mutant (K42E) in the Dimerization Region. Mutation Does Not Alter Oligomerization but Impacts the Heme Iron Spin State and Nitric Oxide Binding Properties-Reference-Cited by-同舟云学术

Heterologous Overexpression and Purification of Cytochrome c‘ from Rhodobacter capsulatus and a Mutant (K42E) in the Dimerization Region. Mutation Does Not Alter Oligomerization but Impacts the Heme Iron Spin State and Nitric Oxide Binding Properties

Published:2006-03-21 Issue:14 Volume:45 Page:4388-4395
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Huston Wilhelmina M.¹,Andrew Colin R.¹,Servid Amy E.¹,McKay Alison L.¹,Leech Andrew P.¹,Butler Clive S.¹,Moir James W. B.¹

Affiliation:

1. Department of Biology (Area 10), University of York, Heslington, York, YO10 5YW, United Kingdom, Institute for Cell and Molecular Biosciences, University of Newcastle, Newcastle upon Tyne, NE2 4HH, United Kingdom, and Department of Chemistry and Biochemistry, Eastern Oregon University, La Grande, Oregon 97850

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi052605j

Reference31 articles.

1. Anomalous Ligand Binding by a Class of High Spin c-Type Cytochromes

2. Nitric Oxide Complex of Cytochrome c' in Cells of Denitrifying Bacteria

3. Cytochrome c ′ from Rhodobacter capsulatus Confers Increased Resistance to Nitric Oxide

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