Soluble domains of cytochrome c -556 and Rieske iron-sulfur protein from Chlorobaculum tepidu m: Crystal structures and interaction analysis.

Autor: Kishimoto H; Department of Biological Sciences, Graduate School of Science, Osaka University, Toyonaka, Osaka, 560-0043, Japan., Azai C; Graduate School of Life Sciences, Ritsumeikan University, Kusatsu, Shiga, 525-8577, Japan., Yamamoto T; Department of Biological Sciences, Graduate School of Science, Osaka University, Toyonaka, Osaka, 560-0043, Japan., Mutoh R; Institute for Protein Research, Osaka University, Suita, Osaka, 565-0871, Japan., Nakaniwa T; Institute for Protein Research, Osaka University, Suita, Osaka, 565-0871, Japan., Tanaka H; Institute for Protein Research, Osaka University, Suita, Osaka, 565-0871, Japan., Miyanoiri Y; Institute for Protein Research, Osaka University, Suita, Osaka, 565-0871, Japan., Kurisu G; Institute for Protein Research, Osaka University, Suita, Osaka, 565-0871, Japan., Oh-Oka H; Department of Biological Sciences, Graduate School of Science, Osaka University, Toyonaka, Osaka, 560-0043, Japan.; Center for Education in Liberal Arts and Sciences, Osaka University, Toyonaka, Osaka, 560-0043, Japan.
Jazyk: angličtina
Zdroj: Current research in structural biology [Curr Res Struct Biol] 2023 Apr 19; Vol. 5, pp. 100101. Date of Electronic Publication: 2023 Apr 19 (Print Publication: 2023).
DOI: 10.1016/j.crstbi.2023.100101
Abstrakt: In photosynthetic green sulfur bacteria, the electron transfer reaction from menaquinol:cytochrome c oxidoreductase to the P840 reaction center (RC) complex occurs directly without any involvement of soluble electron carrier protein(s). X-ray crystallography has determined the three-dimensional structures of the soluble domains of the CT0073 gene product and Rieske iron-sulfur protein (ISP). The former is a mono-heme cytochrome c with an α-absorption peak at 556 nm. The overall fold of the soluble domain of cytochrome c -556 (designated as cyt c -556 sol ) consists of four α-helices and is very similar to that of water-soluble cyt c -554 that independently functions as an electron donor to the P840 RC complex. However, the latter's remarkably long and flexible loop between the α3 and α4 helices seems to make it impossible to be a substitute for the former. The structure of the soluble domain of the Rieske ISP (Rieske sol protein) shows a typical β-sheets-dominated fold with a small cluster-binding and a large subdomain. The architecture of the Rieske sol protein is bilobal and belongs to those of b 6 f -type Rieske ISPs. Nuclear magnetic resonance (NMR) measurements revealed weak non-polar but specific interaction sites on Rieske sol protein when mixed with cyt c -556 sol . Therefore, menaquinol:cytochrome c oxidoreductase in green sulfur bacteria features a Rieske/cyt b complex tightly associated with membrane-anchored cyt c -556.
Competing Interests: The authors declare the following financial interests/personal relationships which may be considered as potential competing interests: Hirozo Oh-oka reports financial support was provided by 10.13039/501100001691Japan Society for the Promotion of Science. Chihiro Azai reports financial support was provided by 10.13039/501100001691Japan Society for the Promotion of Science. Risa Mutoh reports financial support was provided by 10.13039/501100001691Japan Society for the Promotion of Science. Genji Kurisu reports financial support was provided by JST-10.13039/501100003382CREST.
(© 2023 The Authors.)
Databáze: MEDLINE
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