Domain Swapping of the Heme and N-Terminal α-Helix in Hydrogenobacter thermophilus Cytochrome c552 Dimer-Reference-Cited by-同舟云学术

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Domain Swapping of the Heme and N-Terminal α-Helix in Hydrogenobacter thermophilus Cytochrome c552 Dimer

Published:2012-10-18 Issue:43 Volume:51 Page:8608-8616
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Hayashi Yugo¹,Nagao Satoshi¹,Osuka Hisao²,Komori Hirofumi²³,Higuchi Yoshiki²³,Hirota Shun¹

Affiliation:

1. Graduate School of Materials Science, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan

2. Department of Life Science, Graduate School of Life Science, University of Hyogo, 3-2-1 Koto, Kamigori-cho, Ako-gun, Hyogo 678-1297, Japan

3. RIKEN SPring-8 Center, 1-1-1 Koto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi3011303

Reference75 articles.

1. Principles that Govern the Folding of Protein Chains

2. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

3. Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of Pathogenesis

4. Amyloid formation by globular proteins under native conditions

5. Deposition Diseases and 3D Domain Swapping

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1. Construction of ligand-binding controlled hemoprotein assemblies utilizing 3D domain swapping;Chemical Communications;2024

2. Supramolecular assembling systems of hemoproteins using chemical modifications;Journal of Inclusion Phenomena and Macrocyclic Chemistry;2023-03-18

3. Resonance Raman Studies on Heme Ligand Stretching Modes in Methionine80-Depleted Cytochrome c: Fe–His, Fe–O₂, and O–O Stretching Modes;The Journal of Physical Chemistry B;2023-03-15

4. New Aspects of Cytochromec: 3D Domain Swapping, Membrane Interaction, Peroxidase Activity, and Met80 Sulfoxide Modification;Bulletin of the Chemical Society of Japan;2021-01-15

5. Use of 3D domain swapping in constructing supramolecular metalloproteins;Chemical Communications;2021

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