X-ray Absorption Studies on the Mixed-Valence and Fully Reduced Forms of the Soluble CuA Domains of Cytochrome c Oxidase-Reference-Cited by-同舟云学术

X-ray Absorption Studies on the Mixed-Valence and Fully Reduced Forms of the Soluble CuA Domains of Cytochrome c Oxidase

Published:1997-07-01 Issue:26 Volume:119 Page:6135-6143
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Blackburn Ninian J.¹,de Vries Simon¹,Barr Mary E.¹,Houser Robert P.¹,Tolman William B.¹,Sanders Donita¹,Fee James A.¹

Affiliation:

1. Contribution from the Department of Biochemistry and Molecular Biology, Oregon Graduate Institute of Science and Technology, P.O. Box 91000, Portland, Oregon 97291-1000, Department of Microbiology and Enzymology, Technical University of Delft, Julianalaan 67, 2628 BC Delft, The Netherlands, Chemical Sciences and Technology Division, Los Alamos National Laboratory, Mail Stop C345, Los Alamos, New Mexico 87545, Department of Chemistry and Center for Metals in Biocatalysis, University of Minnesota, 207...

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja970513e

Reference72 articles.

1. Insight into the active-site structure and function of cytochrome oxidase by analysis of site-directed mutants of bacterial cytochromeaa 3 and cytochromebo

2. The cytochrome oxidase superfamily of redox-driven proton pumps

3. Definition of the catalytic site of cytochrome c oxidase: specific ligands of heme a and the heme a3-CuB center.

4. Spectroscopic and genetic evidence for two heme-Cu-containing oxidases in Rhodobacter sphaeroides

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