The Reactions of O2 and NO with Mixed-Valence ba3 Cytochrome c Oxidase from Thermus thermophilus

Autor: Istvan Szundi, Ólőf Einarsdóttir, Tewfik Soulimane, Chie Funatogawa

Publikováno v: Biophys J

Earlier CO flow-flash experiments on the fully reduced Thermus thermophilus ba(3) (Tt ba(3)) cytochrome oxidase revealed that O(2) binding was slowed down by a factor of 10 in the presence of CO (Szundi et al., 2010, PNAS 107, 21010–21015). The goa

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ea61750c76879357dddf5ff2d5b8e898
https://doi.org/10.1016/j.bpj.2019.11.3390

Role of the Conserved Valine 236 in Access of Ligands to the Active Site of Thermus thermophilus ba3 Cytochrome Oxidase

Autor: Ying Chen, Yang Li, Ólöf Einarsdóttir, C. David Stout, Chie Funatogawa, Istvan Szundi, William McDonald, James A. Fee

Publikováno v: Biochemistry. 56:107-119

Knowledge of the role of conserved residues in the ligand channel of heme-copper oxidases is critical for understanding how the protein scaffold modulates the function of these enzymes. In this study, we investigated the role of the conserved valine

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::1ebe8c99d26d833d6715c5a587e6d069
https://doi.org/10.1021/acs.biochem.6b00590

A Comparison between the Photoactivation Kinetics of Human and Bovine Rhodopsins

Autor: Chie Funatogawa, Istvan Szundi, David S. Kliger

Publikováno v: Biochemistry, vol 55, iss 50
Funatogawa, C; Szundi, I; & Kliger, DS. (2016). A Comparison between the Photoactivation Kinetics of Human and Bovine Rhodopsins. BIOCHEMISTRY, 55(50), 7005-7013. doi: 10.1021/acs.biochem.6b00953. UC Santa Cruz: Retrieved from: http://www.escholarship.org/uc/item/5r62c2n0

Rhodopsin is a G-protein-coupled receptor important for vertebrate vision under dim light conditions. Many studies of the activation mechanism of bovine rhodopsin have been conducted, but there have been relatively few investigations of the human pro

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3589a6364900e5f277152b62a3fe98e9
https://escholarship.org/uc/item/5r62c2n0

Complexity of Bovine Rhodopsin Activation Revealed at Low Temperature and Alkaline pH

Autor: David S. Kliger, Chie Funatogawa, Istvan Szundi

Publikováno v: Szundi, I; Funatogawa, C; & Kliger, DS. (2016). Complexity of Bovine Rhodopsin Activation Revealed at Low Temperature and Alkaline pH. BIOCHEMISTRY, 55(36), 5095-5105. doi: 10.1021/acs.biochem.6b00687. UC Santa Cruz: Retrieved from: http://www.escholarship.org/uc/item/9mf06051
Biochemistry, vol 55, iss 36

The late intermediates involved in the activation mechanism of bovine rhodopsin are investigated by time-resolved optical absorption spectroscopy. Measurements from 10 μs to 200 ms after photolysis were carried out on membrane suspensions of bovine

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f17601eb5dcbd5ab1e618c45f958d5d
http://www.escholarship.org/uc/item/9mf06051

Spectral identification of intermediates generated during the reaction of dioxygen with the wild-type and EQ(I-286) mutant of Rhodobacter sphaeroides cytochrome c oxidase

Autor: Carrie Hiser, Jennifer A. Cassano, Istvan Szundi, Jayashree Ray, Robert B. Gennis, Ólöf Einarsdóttir, Shelagh Ferguson-Miller, William McDonald, Chie Funatogawa

Publikováno v: Biochemistry. 51(46)

Cytochrome c oxidase from Rhodobacter sphaeroides is frequently used to model the more complex mitochondrial enzyme. The O(2) reduction in both enzymes is generally described by a unidirectional mechanism involving the sequential formation of the fer

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::30db29263d4ba1fa92a962c8786a8ee3
https://pubmed.ncbi.nlm.nih.gov/23057757