Role of the Surface-Exposed Leucine 155 in the Metal Ion Binding Loop of the CuA Domain of Cytochrome c Oxidase from Thermus thermophilus on the Function and Stability of the Protein-Reference-Cited by-同舟云学术

Role of the Surface-Exposed Leucine 155 in the Metal Ion Binding Loop of the CuA Domain of Cytochrome c Oxidase from Thermus thermophilus on the Function and Stability of the Protein

Published:2012-03-12 Issue:12 Volume:51 Page:2443-2452
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Ghosh Manas Kumar¹,Rajbongshi Jitumani¹²,Basumatary Debajani¹,Mazumdar Shyamalava¹

Affiliation:

1. Department of Chemical Sciences, Tata Institute of Fundamental Research, Colaba, Mumbai 400005, India

2. Department of Chemistry, Gauhati University, Guwahati 781014, India

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi2017574

Reference37 articles.

1. Cytochrome c oxidase: understanding nature's design of a proton pump

2. The Whole Structure of the 13-Subunit Oxidized Cytochrome c Oxidase at 2.8 Å

3. Crystal structure of the membrane-exposed domain from a respiratory quinol oxidase complex with an engineered dinuclear copper center.

4. Structure at 2.7 A resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody FV fragment

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