The Rubredoxin from Clostridium pasteurianum: Mutation of the Iron Cysteinyl Ligands to Serine. Crystal and Molecular Structures of Oxidized and Dithionite-Treated Forms of the Cys42Ser Mutant-Reference-Cited by-同舟云学术

The Rubredoxin from Clostridium pasteurianum: Mutation of the Iron Cysteinyl Ligands to Serine. Crystal and Molecular Structures of Oxidized and Dithionite-Treated Forms of the Cys42Ser Mutant

Published:1998-04-17 Issue:17 Volume:120 Page:4135-4150
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Xiao Zhiguang¹,Lavery Megan J.¹,Ayhan Mustafa¹,Scrofani Sergio D. B.¹,Wilce Matthew C. J.¹,Guss J. Mitchell¹,Tregloan Peter A.¹,George Graham N.¹,Wedd Anthony G.¹

Affiliation:

1. Contribution from the School of Chemistry, University of Melbourne, Parkville, Victoria 3052, Australia, Department of Biochemistry, University of Sydney, Sydney, New South Wales 2006, Australia, and Stanford Synchrotron Radiation Laboratory, SLAC, Stanford University, P.O. Box 4349, MS 69, Stanford, California 94309

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja973162c

Reference112 articles.

1. Iron-Sulfur Clusters: Nature's Modular, Multipurpose Structures

2. [15] Characterization of three proteins containing multiple iron sites: Rubrerythrin, desulfoferrodoxin, and a protein containing a six-iron cluster

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